[ CAS No. 132327-80-1 ] Fmoc-Gln(Trt)-OH

Cat. No.: A213511

2D 3D

Structure of 132327-80-1 * Storage: Inert atmosphere,Room Temperature

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* Storage: Inert atmosphere,Room Temperature

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Quality Control of [ 132327-80-1 ]

COA NMR CNMR HPLC LC-MS

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Specification

Alternatived Products of [ 132327-80-1 ]

Product Details of [ 132327-80-1 ]

CAS No. :	132327-80-1	MDL No. :	MFCD00077056
Formula :	C₃₉H₃₄N₂O₅	Boiling Point :	-
Linear Structure Formula :	C₁₅H₁₀O₂C₄H₇N₂O₃C(C₆H₅)₃CH₂	InChI Key :	WDGICUODAOGOMO-DHUJRADRSA-N
M.W :	610.70	Pubchem ID :	10919157
Synonyms :

Calculated chemistry of [ 132327-80-1 ] Expand+

Safety of [ 132327-80-1 ]

Signal Word:	Warning	Class:	N/A
Precautionary Statements:	P280	UN#:	N/A
Hazard Statements:	H317-H413	Packing Group:	N/A
GHS Pictogram:

Application In Synthesis of [ 132327-80-1 ]

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

Downstream synthetic route of [ 132327-80-1 ]

[ 132327-80-1 ] Synthesis Path-Downstream 1~21

1
[ 29022-11-5 ]
[ 35661-40-6 ]
[ 108-24-7 ]
[ 132327-80-1 ]
[ 198561-07-8 ]
Ac-Gln-Asp-Phe-Gly-OH [ No CAS ]

Reference： [1]Organic Letters,2007,vol. 9,p. 2469 - 2472

2
Fmoc-Rink resin [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 96402-49-2 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
C₁₃₁H₁₇₆N₁₉O₂₂PolS [ No CAS ]

Reference： [1]Journal of the American Chemical Society,2008,vol. 130,p. 14625 - 14633

3
Fmoc-Rink resin [ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 96402-49-2 ]
[ 118358-38-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
C₁₄₁H₁₈₆N₁₉O₃₁PolS [ No CAS ]

Reference： [1]Journal of the American Chemical Society,2008,vol. 130,p. 14625 - 14633

4
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 71989-28-1 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
H-(propargylglycyl)-QGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIA-NH₂ [ No CAS ]

Reference： [1]Journal of Peptide Science,2011,vol. 17,p. 270 - 280

5
C₂₃H₂₂NO₆Pol [ No CAS ]
C₁₇H₃₅NO₅Si [ No CAS ]
[ 35661-60-0 ]
[ 132327-80-1 ]
[ 77128-73-5 ]
[ 71989-33-8 ]
[ 56-40-6 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
N-FMOC-O-tert-butyl-D-threonine [ No CAS ]
Fmoc-D-Ile-OH [ No CAS ]
C₇₅H₁₁₆N₂₀O₂₀ [ No CAS ]

Reference： [1]Angewandte Chemie - International Edition,2015,vol. 54,p. 1556 - 1560
Angew. Chem.,2015,vol. 127,p. 1576 - 1580,5

6
[ 29022-11-5 ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
[ 58-85-5 ]
[ 198561-07-8 ]
C₆₆H₉₄N₂₀O₂₁S [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: 4.1.1. Peptide synthesis; 4.1.2; Solid-phase peptide synthesis (SPPS) was performed with standardFmoc chemistry on rink amide resin using an automated peptidesynthesizer (Syro I, Multisyntech). The resin was loaded into a5 mL reactor with a frit at the bottom. Swelling was performed bydispensing 1 mL DMF and incubating for 15 min (2) with 10 sshaking every minute. Fmoc deprotection was achieved by treatmentwith 40percent piperidine DMF for 3 min and 20percent piperidine inDMF for 12 min (10 s/min shaking). Peptide couplings were carriedout by double couplings with Fmoc-protected amino acids(5 equiv), HBTU (5 equiv), HOBt (5 equiv) and DIPEA (10 equiv) inDMF for 40 min (10 s/min shaking). At the respective position,Fmoc-F2Pmp-OH (3 equiv) was coupled in DMF (1 mL) by manualaddition using TBTU (3 equiv), HOBt (3 equiv) and DIPEA (6 equiv)for 3 h, after 3 min preactivation. In case of the sequences for which side-chain labeling with biotinor carboxyfluorescein was planned, an additional 4-methyltrityl-(Mtt-) protected lysine was coupled to the N-terminus. Toselectively remove the Mtt group the resin was washed for 1 minwith DCM (3), deprotection was then achieved by treatment with1.8percent TFA in DCM for 3 min (10). During the deprotection the DCMsolution turned yellow.For fluorescein-labeling of the amine side-chain 5(6)-carboxyfluorescein(3 equiv), HATU (3 equiv), HOAt (3 equiv) andDIPEA (6 equiv) were dissolved in DMF and pre-activated for3 min. The solution was aspirated and coupling was allowed toproceed for 1 h. This step was repeated 4 times.For biotin-labeling of the amine side-chain the resin waswashed for 1 min in NMP (3). D-(+)-Biotin (3 equiv), HATU(3 equiv), HOAt (3 equiv) and DIPEA (6 equiv) were dissolved inNMP and pre-activated for 3 min. The solution was aspirated andcoupling was allowed to proceed for 2 h. This step was repeated2 times. N-terminal acetylation (where applicable) was achieved by dispensing800 lL of a mixture of acetic anhydride/pyridine (1:9) andreaction twice for 5 min (10 s/min shaking). After each deprotection,coupling or acetylation step, 5 washings (1 min each) withDMF were performed (10 s/min shaking).After synthesis the resin was transferred in a 5 mL syringeequipped with a frit, washed with DCM for 1 min (3) and driedin high vacuum for at least 30 min. For cleavage 1 mL of a mixtureof TFA and TIS (20:1) was added. The syringe with the mixture waskept on a shaker for 3 h. Then the liquid phase was filtered into20 mL of ice-cold Et2O. Formed precipitate was centrifuged,washed with ice-cold Et2O (2 20 mL) and purified by HPLC. 4.1.2. Azide functionalization of the N-terminus; To the peptides with the longer carbon linker, 6-azidohexanoicacid was coupled (with standard coupling conditions) to the Nterminalamine.The N-terminal amine of the peptides with the shorter linkerwas converted to an azide functionality directly on solid support.Using the compound imidazole-1-sulfonyl-azideHCl (synthesissee beneath) and modified conditions, which were reported forsolution phase chemistry from Goddard?Borger and Stick:8 Theresin was washed for 1 min each with DCM (2), DCM/MeOH(2) and MeOH (3). Then (for 40 mg resin, loading= 0.62 mmole/g) 1.4 equiv of imidazole-1-sulfonyl-azideHClin 1 mL MeOH and 100 ll of a saturated and centrifuged solutionof CuSO4*5H2O was added. After 1 min, DIPEA (1.8 equiv) wasadded and the coupling was allowed to proceed for 1 h andrepeated once more with an intermediate washing with MeOH(3 1 min).

Reference： [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 2848 - 2853

7
[ 79598-53-1 ]
[ 29022-11-5 ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 71989-38-3 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
[ 58-85-5 ]
[ 198561-07-8 ]
C₇₂H₁₀₅N₂₁O₂₂S [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: 4.1.1. Peptide synthesis; 4.1.2; Solid-phase peptide synthesis (SPPS) was performed with standardFmoc chemistry on rink amide resin using an automated peptidesynthesizer (Syro I, Multisyntech). The resin was loaded into a5 mL reactor with a frit at the bottom. Swelling was performed bydispensing 1 mL DMF and incubating for 15 min (2) with 10 sshaking every minute. Fmoc deprotection was achieved by treatmentwith 40percent piperidine DMF for 3 min and 20percent piperidine inDMF for 12 min (10 s/min shaking). Peptide couplings were carriedout by double couplings with Fmoc-protected amino acids(5 equiv), HBTU (5 equiv), HOBt (5 equiv) and DIPEA (10 equiv) inDMF for 40 min (10 s/min shaking). At the respective position,Fmoc-F2Pmp-OH (3 equiv) was coupled in DMF (1 mL) by manualaddition using TBTU (3 equiv), HOBt (3 equiv) and DIPEA (6 equiv)for 3 h, after 3 min preactivation. In case of the sequences for which side-chain labeling with biotinor carboxyfluorescein was planned, an additional 4-methyltrityl-(Mtt-) protected lysine was coupled to the N-terminus. Toselectively remove the Mtt group the resin was washed for 1 minwith DCM (3), deprotection was then achieved by treatment with1.8percent TFA in DCM for 3 min (10). During the deprotection the DCMsolution turned yellow.For fluorescein-labeling of the amine side-chain 5(6)-carboxyfluorescein(3 equiv), HATU (3 equiv), HOAt (3 equiv) andDIPEA (6 equiv) were dissolved in DMF and pre-activated for3 min. The solution was aspirated and coupling was allowed toproceed for 1 h. This step was repeated 4 times.For biotin-labeling of the amine side-chain the resin waswashed for 1 min in NMP (3). D-(+)-Biotin (3 equiv), HATU(3 equiv), HOAt (3 equiv) and DIPEA (6 equiv) were dissolved inNMP and pre-activated for 3 min. The solution was aspirated andcoupling was allowed to proceed for 2 h. This step was repeated2 times. N-terminal acetylation (where applicable) was achieved by dispensing800 lL of a mixture of acetic anhydride/pyridine (1:9) andreaction twice for 5 min (10 s/min shaking). After each deprotection,coupling or acetylation step, 5 washings (1 min each) withDMF were performed (10 s/min shaking).After synthesis the resin was transferred in a 5 mL syringeequipped with a frit, washed with DCM for 1 min (3) and driedin high vacuum for at least 30 min. For cleavage 1 mL of a mixtureof TFA and TIS (20:1) was added. The syringe with the mixture waskept on a shaker for 3 h. Then the liquid phase was filtered into20 mL of ice-cold Et2O. Formed precipitate was centrifuged,washed with ice-cold Et2O (2 20 mL) and purified by HPLC. 4.1.2. Azide functionalization of the N-terminus; To the peptides with the longer carbon linker, 6-azidohexanoicacid was coupled (with standard coupling conditions) to the Nterminalamine.The N-terminal amine of the peptides with the shorter linkerwas converted to an azide functionality directly on solid support.Using the compound imidazole-1-sulfonyl-azideHCl (synthesissee beneath) and modified conditions, which were reported forsolution phase chemistry from Goddard?Borger and Stick:8 Theresin was washed for 1 min each with DCM (2), DCM/MeOH(2) and MeOH (3). Then (for 40 mg resin, loading= 0.62 mmole/g) 1.4 equiv of imidazole-1-sulfonyl-azideHClin 1 mL MeOH and 100 ll of a saturated and centrifuged solutionof CuSO4*5H2O was added. After 1 min, DIPEA (1.8 equiv) wasadded and the coupling was allowed to proceed for 1 h andrepeated once more with an intermediate washing with MeOH(3 1 min).

Reference： [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 2848 - 2853

8
[ 29022-11-5 ]
Fmoc-F₂Pmp-OH [ No CAS ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
[ 58-85-5 ]
[ 198561-07-8 ]
C₆₇H₉₅F₂N₂₀O₂₃PS [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: 4.1.1. Peptide synthesis; 4.1.2; Solid-phase peptide synthesis (SPPS) was performed with standardFmoc chemistry on rink amide resin using an automated peptidesynthesizer (Syro I, Multisyntech). The resin was loaded into a5 mL reactor with a frit at the bottom. Swelling was performed bydispensing 1 mL DMF and incubating for 15 min (2) with 10 sshaking every minute. Fmoc deprotection was achieved by treatmentwith 40percent piperidine DMF for 3 min and 20percent piperidine inDMF for 12 min (10 s/min shaking). Peptide couplings were carriedout by double couplings with Fmoc-protected amino acids(5 equiv), HBTU (5 equiv), HOBt (5 equiv) and DIPEA (10 equiv) inDMF for 40 min (10 s/min shaking). At the respective position,Fmoc-F2Pmp-OH (3 equiv) was coupled in DMF (1 mL) by manualaddition using TBTU (3 equiv), HOBt (3 equiv) and DIPEA (6 equiv)for 3 h, after 3 min preactivation. In case of the sequences for which side-chain labeling with biotinor carboxyfluorescein was planned, an additional 4-methyltrityl-(Mtt-) protected lysine was coupled to the N-terminus. Toselectively remove the Mtt group the resin was washed for 1 minwith DCM (3), deprotection was then achieved by treatment with1.8percent TFA in DCM for 3 min (10). During the deprotection the DCMsolution turned yellow.For fluorescein-labeling of the amine side-chain 5(6)-carboxyfluorescein(3 equiv), HATU (3 equiv), HOAt (3 equiv) andDIPEA (6 equiv) were dissolved in DMF and pre-activated for3 min. The solution was aspirated and coupling was allowed toproceed for 1 h. This step was repeated 4 times.For biotin-labeling of the amine side-chain the resin waswashed for 1 min in NMP (3). D-(+)-Biotin (3 equiv), HATU(3 equiv), HOAt (3 equiv) and DIPEA (6 equiv) were dissolved inNMP and pre-activated for 3 min. The solution was aspirated andcoupling was allowed to proceed for 2 h. This step was repeated2 times. N-terminal acetylation (where applicable) was achieved by dispensing800 lL of a mixture of acetic anhydride/pyridine (1:9) andreaction twice for 5 min (10 s/min shaking). After each deprotection,coupling or acetylation step, 5 washings (1 min each) withDMF were performed (10 s/min shaking).After synthesis the resin was transferred in a 5 mL syringeequipped with a frit, washed with DCM for 1 min (3) and driedin high vacuum for at least 30 min. For cleavage 1 mL of a mixtureof TFA and TIS (20:1) was added. The syringe with the mixture waskept on a shaker for 3 h. Then the liquid phase was filtered into20 mL of ice-cold Et2O. Formed precipitate was centrifuged,washed with ice-cold Et2O (2 20 mL) and purified by HPLC. 4.1.2. Azide functionalization of the N-terminus; To the peptides with the longer carbon linker, 6-azidohexanoicacid was coupled (with standard coupling conditions) to the Nterminalamine.The N-terminal amine of the peptides with the shorter linkerwas converted to an azide functionality directly on solid support.Using the compound imidazole-1-sulfonyl-azideHCl (synthesissee beneath) and modified conditions, which were reported forsolution phase chemistry from Goddard?Borger and Stick:8 Theresin was washed for 1 min each with DCM (2), DCM/MeOH(2) and MeOH (3). Then (for 40 mg resin, loading= 0.62 mmole/g) 1.4 equiv of imidazole-1-sulfonyl-azideHClin 1 mL MeOH and 100 ll of a saturated and centrifuged solutionof CuSO4*5H2O was added. After 1 min, DIPEA (1.8 equiv) wasadded and the coupling was allowed to proceed for 1 h andrepeated once more with an intermediate washing with MeOH(3 1 min).

Reference： [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 2848 - 2853

9
[ 79598-53-1 ]
[ 29022-11-5 ]
Fmoc-F₂Pmp-OH [ No CAS ]
[ 71989-31-6 ]
[ 71989-18-9 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid [ No CAS ]
[ 58-85-5 ]
[ 198561-07-8 ]
C₇₃H₁₀₆F₂N₂₁O₂₄PS [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		General procedure: 4.1.1. Peptide synthesis; 4.1.2; Solid-phase peptide synthesis (SPPS) was performed with standardFmoc chemistry on rink amide resin using an automated peptidesynthesizer (Syro I, Multisyntech). The resin was loaded into a5 mL reactor with a frit at the bottom. Swelling was performed bydispensing 1 mL DMF and incubating for 15 min (2) with 10 sshaking every minute. Fmoc deprotection was achieved by treatmentwith 40percent piperidine DMF for 3 min and 20percent piperidine inDMF for 12 min (10 s/min shaking). Peptide couplings were carriedout by double couplings with Fmoc-protected amino acids(5 equiv), HBTU (5 equiv), HOBt (5 equiv) and DIPEA (10 equiv) inDMF for 40 min (10 s/min shaking). At the respective position,Fmoc-F2Pmp-OH (3 equiv) was coupled in DMF (1 mL) by manualaddition using TBTU (3 equiv), HOBt (3 equiv) and DIPEA (6 equiv)for 3 h, after 3 min preactivation. In case of the sequences for which side-chain labeling with biotinor carboxyfluorescein was planned, an additional 4-methyltrityl-(Mtt-) protected lysine was coupled to the N-terminus. Toselectively remove the Mtt group the resin was washed for 1 minwith DCM (3), deprotection was then achieved by treatment with1.8percent TFA in DCM for 3 min (10). During the deprotection the DCMsolution turned yellow.For fluorescein-labeling of the amine side-chain 5(6)-carboxyfluorescein(3 equiv), HATU (3 equiv), HOAt (3 equiv) andDIPEA (6 equiv) were dissolved in DMF and pre-activated for3 min. The solution was aspirated and coupling was allowed toproceed for 1 h. This step was repeated 4 times.For biotin-labeling of the amine side-chain the resin waswashed for 1 min in NMP (3). D-(+)-Biotin (3 equiv), HATU(3 equiv), HOAt (3 equiv) and DIPEA (6 equiv) were dissolved inNMP and pre-activated for 3 min. The solution was aspirated andcoupling was allowed to proceed for 2 h. This step was repeated2 times. N-terminal acetylation (where applicable) was achieved by dispensing800 lL of a mixture of acetic anhydride/pyridine (1:9) andreaction twice for 5 min (10 s/min shaking). After each deprotection,coupling or acetylation step, 5 washings (1 min each) withDMF were performed (10 s/min shaking).After synthesis the resin was transferred in a 5 mL syringeequipped with a frit, washed with DCM for 1 min (3) and driedin high vacuum for at least 30 min. For cleavage 1 mL of a mixtureof TFA and TIS (20:1) was added. The syringe with the mixture waskept on a shaker for 3 h. Then the liquid phase was filtered into20 mL of ice-cold Et2O. Formed precipitate was centrifuged,washed with ice-cold Et2O (2 20 mL) and purified by HPLC. 4.1.2. Azide functionalization of the N-terminus; To the peptides with the longer carbon linker, 6-azidohexanoicacid was coupled (with standard coupling conditions) to the Nterminalamine.The N-terminal amine of the peptides with the shorter linkerwas converted to an azide functionality directly on solid support.Using the compound imidazole-1-sulfonyl-azideHCl (synthesissee beneath) and modified conditions, which were reported forsolution phase chemistry from Goddard?Borger and Stick:8 Theresin was washed for 1 min each with DCM (2), DCM/MeOH(2) and MeOH (3). Then (for 40 mg resin, loading= 0.62 mmole/g) 1.4 equiv of imidazole-1-sulfonyl-azideHClin 1 mL MeOH and 100 ll of a saturated and centrifuged solutionof CuSO4*5H2O was added. After 1 min, DIPEA (1.8 equiv) wasadded and the coupling was allowed to proceed for 1 h andrepeated once more with an intermediate washing with MeOH(3 1 min).

Reference： [1]Bioorganic and Medicinal Chemistry,2015,vol. 23,p. 2848 - 2853

10
polyethylene glycol polyamide resin [ No CAS ]
[ 29022-11-5 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
Palm-γGlu-γGlu-OSu [ No CAS ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 71989-35-0 ]
[ 132327-80-1 ]
[ 71989-33-8 ]
[ 94744-50-0 ]
[ 32926-43-5 ]
[ 143824-78-6 ]
[ 204777-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
H-dSer-Q-G-T-F-T-S-D-L-S-K-Q-K((S)-4-carboxy-4-((S)-4-carboxy-4-hexadecanoylamino-butyrylamino)butyryl)-D-E-E-A-A-R-L-F-I-E-W-L-Aib-A-G-G-P-S-S-G-A-P-P-P-S-NH₂ [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
		The solid phase synthesis as described in Methods was carried out on Novabiochem Rink-Amide resin (4-(2',4'-Dimethoxyphenyl-Fmoc-aminomethyl)-phenoxyacetamido- norleucylaminomethyl resin), 100-200 mesh, loading of 0.23 mmol/g. The Fmoc- synthesis strategy was applied with HBTU/DIPEA-activation. In position 14 Fmoc- Lys(ivDde)-OH and in position 1 Boc-His(Trt)-OH were used in the solid phase synthesis protocol. The ivDde-group was cleaved from the peptide on resin according to literature (S.R. Chhabra et al., Tetrahedron Lett. 39, (1998), 1603). Hereafter Palm- yGlu-yGlu-OSu was coupled to the liberated amino-group employing DIPEA as base. The peptide was cleaved from the resin with King's cocktail (D. S. King, C. G. Fields, G. B. Fields, Int. J. Peptide Protein Res. 36, 1990, 255-266). The crude product was purified via preparative HPLC on a Waters column (XBridge, BEH130, Prep C18 5muMu) using an acetonitrile/water gradient (both buffers with 0,1 percent TFA). The purified peptide was analysed by LCMS (Method A). Deconvolution of the mass signals found under the peak with retention time 12.61 min revealed the peptide mass 4581 ,5 which is in line with the expected value of 4581 ,1 . Peptide Synthesizer (Protein Technologies Inc) or similar automated synthesizer using standard Fmoc chemistry and HBTU/DIPEA activation. DMF was used as the solvent. Deprotection : 20percent piperidine/DMF for 2 x 2.5 min. Washes: 7 x DMF. Coupling 2:5:10 200 mM AA / 500 mM HBTU / 2M DIPEA in DMF 2 x for 20 min. Washes: 5 x DMF. In cases where a Lys-side-chain was modified, Fmoc-L-Lys(ivDde)-OH or Fmoc-L- Lys(Mmt)-OH was used in the corresponding position. After completion of the synthesis, the ivDde group was removed according to a modified literature procedure (S.R. Chhabra et al., Tetrahedron Lett. 39, (1998), 1603), using 4percent hydrazine hydrate in DMF. The Mmt group was removed by repeated treatment with 1 percent TFA in dichloromethane. The following acylations were carried out by treating the resin with the N-hydroxy succinimide esters of the desired acid or using coupling reagents like HBTU/DIPEA or HOBt/DIC. All the peptides that have been synthesized were cleaved from the resin with King's cleavage cocktail consisting of 82.5percent TFA, 5percent phenol, 5percent water, 5percent thioanisole, 2.5percent EDT The crude peptides were then precipitated in diethyl or diisopropyl ether, centrifuged, and lyophilized. Peptides were analyzed by analytical HPLC and checked by ESI mass spectrometry. Crude peptides were purified by a conventional preparative RP-HPLC purification procedure.

Reference： [1]Patent: WO2015/155140,2015,A1 .Location in patent: Page/Page column 44; 45; 53

11
[ 35661-60-0 ]
[ 35661-39-3 ]
Boc-His(Trt)-Gly-Asp(tBu)-Gly-OH [ No CAS ]
[ 35661-40-6 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 96402-49-2 ]
[ 77284-32-3 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
Fmoc-Thr(Pg)-OH [ No CAS ]
Fmoc-Ser(Pg)-OH [ No CAS ]
C₁₆₀H₂₃₇N₄₁O₄₇ [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2016,vol. 59,p. 3129 - 3139

12
[ 35661-60-0 ]
[ 35661-39-3 ]
Boc-His(Trt)-Gly-Asp(tBu)-Gly-OH [ No CAS ]
[ 35661-40-6 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 77284-32-3 ]
[ 32926-43-5 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
Fmoc-Thr(Pg)-OH [ No CAS ]
Fmoc-Ser(Pg)-OH [ No CAS ]
C₁₅₃H₂₃₃N₄₃O₄₇ [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2016,vol. 59,p. 3129 - 3139

13
[ 35661-60-0 ]
[ 35661-39-3 ]
Boc-His(Trt)-Gly-Asp(tBu)-Gly-OH [ No CAS ]
[ 35661-40-6 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 77284-32-3 ]
[ 32926-43-5 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
Fmoc-Thr(Pg)-OH [ No CAS ]
Fmoc-Ser(Pg)-OH [ No CAS ]
C₁₅₃H₂₃₃N₄₃O₄₇ [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2016,vol. 59,p. 3129 - 3139

14
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 35661-40-6 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-26-9 ]
[ 35661-38-2 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 77284-32-3 ]
[ 32926-43-5 ]
[ 143824-78-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
Fmoc-Thr(Pg)-OH [ No CAS ]
Fmoc-Ser(Pg)-OH [ No CAS ]
C₁₅₂H₂₃₄N₄₂O₄₈ [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2016,vol. 59,p. 3129 - 3139

15
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
N⁴-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-N²-(9-fluorenylmethylcarbonyl)asparagine [ No CAS ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 109425-51-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
KCNTATCATQRLANFLVHSS-(α-propargylglycinyl)-NFGPILPPTNVGS-(N⁴-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)asparaginyl)-TY-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2016,vol. 14,p. 5238 - 5245

16
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
N⁴-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-N²-(9-fluorenylmethylcarbonyl)asparagine [ No CAS ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 109425-51-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
KCNTATCATQRLANFLVHSS-(N⁴-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)asparaginyl)-NFGPILPPTNVGS-(α-propargylglycinyl)-TY-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2016,vol. 14,p. 5238 - 5245

17
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 109425-51-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
K-CNTATCATQRLANFLVHSSNNFGPILPPTNVGS-(α-propargylglycinyl)-TY-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2016,vol. 14,p. 5238 - 5245

18
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 109425-51-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
K-CNTATCATQRLANFLVHSS-(α-propargylglycinyl)-NFGPILPPTNVGS-(α-propargylglycinyl)-TY-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2016,vol. 14,p. 5238 - 5245

19
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 109425-51-6 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 198561-07-8 ]
KCNTATCATQRLANFLVHSS-(α-propargylglycinyl)-NFGPILPPTNVGSNTY-NH₂ [ No CAS ]

Reference： [1]Organic and Biomolecular Chemistry,2016,vol. 14,p. 5238 - 5245

20
[ 103213-32-7 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 96402-49-2 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
C₄₆H₇₂N₁₈O₁₁S₄ [ No CAS ]

Reference： [1]Journal of Medicinal Chemistry,2016,vol. 59,p. 2381 - 2395

21
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 35661-39-3 ]
[ 864876-97-1 ]
[ 71989-31-6 ]
[ 71989-14-5 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 150629-67-7 ]
[ 125238-99-5 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
[ 58-85-5 ]
NH₂-NK(Biotin)VPNLRGDLQVLAQ[diaminobutyric acid]VART-OH [ No CAS ]

Yield	Reaction Conditions	Operation in experiment
29%		(0234) To enable investigation of introducing non-proteinogenic amino acids (listed in Figure 1) on A20FMDV2 binding activity, biotinylated peptides 1-15 (see Table 1), except for peptide 6, were synthesised by standard Fmoc SPPS on the acid liable (0235) hydroxymethylphenoxypropionic acid linker (HMPP) which delivers a C- terminal carboxylic acid using to the conditions depicted in Scheme 1. The desired peptide sequences were assembled using 20percent (0236) piperidine/DMF to remove the Fmoc protecting group and 0- (0237) (benzotriazol-l-yl) -N, N, N ' , N '-tetramethyluronium hexafluorophosphate (HBTU) / DIPEA as coupling reagents. (0238) Since specific binding to the nubetabeta integrin was to be studied by flow cytometry, the native alanine at the second residue in A20FMDV2 (1) and all analogues thereof, were substituted with a biotinylated lysine residue. This substitution has previously been shown to be well tolerated [24,25] . We chose to install the D-biotin moiety by selective deprotection of a 1- ( 4 , 4-dimethyl-2 , 6-dioxocyclohex-l- ylidene ) ethyl (Dde) [19] group on the side chain group followed by condensation with D-biotin using HBTU/DIPEA. (0239) Trifluoroacetic acid (TFA) /H2O/3, 6-dioxa-l , 8-octanedithiol (0240) (DODT) /triisopropylsilane (TIPS) (94:2.5:2.5:1.0, v/v/v/v) effected cleavage of the synthesised peptides from the corresponding (0241) peptidyl-resins . Peptides 1-15 were obtained in good yields ranging from 2percent-50percent and purity exceeding 99percent (see peptide characterization data) . (0242) For the synthesis of peptide 6 containing an i\7-L-methyllysine modification we employed an on-resin i\7-methylation protocol [22] which furnished peptide 6 in good yield (30percent) following TFA-mediated peptide cleavage and RP-HPLC purification. (0243) The lead peptide, A20FMDV2, which contains all naturally-occurring amino acids would be susceptible to degradation by exopeptidases which act on the amino- and carboxy terminuses. To mitigate this, six N- and/or C-terminus-modified and biotinylated A20FDMV2 mimics were prepared wherein we systematically modified the amino and carboxy ends (peptides 16-18) and the N-terminal and C-terminal amino acids (Asnl and Thr20, respectively, peptides 19-21) . N- terminal/C-terminal modified peptides 16-18 were obtained by capping of the N-terminus with acetic anhydride (16) or by employing the Rink amide linker to afford the C-terminal carboxamide (17) or a combination of both (peptide 18) . (0244) Peptide 19, bearing the unnatural D-Asnl in place of the native Asnl at the N-terminus of biotinylated A20FMDV2 (1) was obtained using the synthetic route outlined in Scheme 1 except that the Fmoc-D- Asn(Trt)-OH building block was incorporated into the synthesis as the N-terminal residue. For the preparation of peptides 20 and 21, which contains the unnatural D-Thr at the C-terminus, HMP-anchored resin 27 (see Scheme 1, HMP = hydroxymethylphenoxyacetic acid) was first esterified with Fmoc-D-Thr (tBu) -OH using DIC/DMAP and the sequence then elongated by Fmoc SPPS . (0245) Table 1. List of prepared synthetic peptides [N-term] - XiK (Biotin) VPNLRGDLQVX2AQX3VARX4- [C-term] containing substitutions for the native Lysl6 (peptides 2-6) or Leul3 (peptides 7-15), C- terminal/N-terminal variants (peptides 16-21) and DTPA-modified peptides (22-26) . NB: nomenclature, particularly X position (0246) numbering used in this table is not the same as that used in the claims . (0247) Compound N- Xl X2 X3 X4 C- term. term. (0248) 1 NH2 Asn Leu Lys Thr C02H (0249) 2 NH2 Asn Leu D-Lys Thr C02H (0250) 3 NH2 Asn Leu L-Orn Thr C02H (0251) 1-2,4- (0252) 4 NH2 Asn Leu diaminobutyric Thr C02H acid (0253) 1-2,3- (0254) 5 NH2 Asn Leu diaminopropionic Thr C02H acid (0255) 6 NH2 Asn Leu ZV-L-meth llysine Thr C02H (0256) 7 NH2 Asn aminoisobutyric Lys Thr C02H acid (0257) 8 NH2 Asn L-norvaline Lys Thr C02H (0258) 9 NH2 Asn L-norleucine Lys Thr C02H (0259) 10 NH2 Asn L-allylglycine Lys Thr C02H (0260) L-tert- (0261) 11 NH2 Asn Lys Thr C02H butylalanine (0262) 12 NH2 Asn L-homoleucine Lys Thr C02H (0263) L-2-amino-3- (0264) 13 NH2 Asn ethylpentanoic Lys Thr C02H acid (0265) L- (0266) 14 NH2 Asn Lys Thr C02H cyclohexylalanine (0267) 15 L- (0268) NH2 Asn Lys Thr C02H adamantylglycine (0269) 16 Ac-NH Asn Leu Lys Thr C02H (0270) 17 NH2 Asn Leu Lys Thr CONH2 (0271) 18 Ac-NH Asn Leu Lys Thr CONH2 (0272) 19 D- (0273) NH2 Leu Lys Thr C02H (0274) Asn (0275) 20 D- (0276) NH2 Asn Leu Lys C02H (0277) Thr (0278) 21 D- D- (0279) NH2 Leu Lys C02H (0280) Asn Thr (0281) 22 DTPA- (0282) Asn Leu Lys Thr C02H NH (0283) 23 DTPA- (0284) Asn Leu Lys Thr C02H Gly-NH (0285) 24 DTPA- (0286) Asn Leu Lys Thr CONH2 NH (0287) 25 DTPA- D- (0288) Leu Lys Thr C02H NH Asn (0289) 26 DTPA- D- D- (0290) Leu Lys C02H NH Asn Thr (0291) 1 D -yrpercent \?Q ^ (0292) ? -^H Q ? (0293) (0294) Scheme 1. Synthetic protocol for the preparation of the biotinylated A20FMDV2 peptide variants. (0295) The results obtained from th...

Reference： [1]Patent: WO2018/197490,2018,A1 .Location in patent: Page/Page column 21-25; 32-37

Recommend Products

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P301 + P310	IF SWALLOWED: Immediately call a POISON CENTER or doctor/physician.
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Num. heavy atoms :	46
Num. arom. heavy atoms :	30
Fraction Csp3 :	0.15
Num. rotatable bonds :	14
Num. H-bond acceptors :	5.0
Num. H-bond donors :	3.0
Molar Refractivity :	175.94
TPSA :	104.73 Å²

GI absorption :	Low
BBB permeant :	No
P-gp substrate :	No
CYP1A2 inhibitor :	No
CYP2C19 inhibitor :	Yes
CYP2C9 inhibitor :	Yes
CYP2D6 inhibitor :	Yes
CYP3A4 inhibitor :	No
Log Kp (skin permeation) :	-5.08 cm/s

Log Po/w (iLOGP) :	3.56
Log Po/w (XLOGP3) :	6.97
Log Po/w (WLOGP) :	6.76
Log Po/w (MLOGP) :	4.57
Log Po/w (SILICOS-IT) :	6.64
Consensus Log Po/w :	5.7

Lipinski :	2.0
Ghose :	None
Veber :	1.0
Egan :	1.0
Muegge :	2.0
Bioavailability Score :	0.56

Log S (ESOL) :	-7.58
Solubility :	0.0000162 mg/ml ; 0.0000000265 mol/l
Class :	Poorly soluble
Log S (Ali) :	-8.98
Solubility :	0.000000635 mg/ml ; 0.000000001 mol/l
Class :	Poorly soluble
Log S (SILICOS-IT) :	-12.62
Solubility :	0.0000000001 mg/ml ; 0.0 mol/l
Class :	Insoluble

[ CAS No. 132327-80-1 ] Fmoc-Gln(Trt)-OH

Quality Control of [ 132327-80-1 ]

Related Doc. of [ 132327-80-1 ]

Product Details of [ 132327-80-1 ]

Calculated chemistry of [ 132327-80-1 ] Expand+

Physicochemical Properties

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Lipophilicity

Druglikeness

Water Solubility

Medicinal Chemistry

Safety of [ 132327-80-1 ]

Application In Synthesis of [ 132327-80-1 ]

[ 132327-80-1 ] Synthesis Path-Downstream 1~21

Technical Information

Precautionary Statements-General

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Storage

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Health hazards

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PAINS :	0.0 alert
Brenk :	0.0 alert
Leadlikeness :	3.0
Synthetic accessibility :	5.18

Physical hazards
Code	Phrase
H200	Unstable explosive
H201	Explosive; mass explosion hazard
H202	Explosive; severe projection hazard
H203	Explosive; fire, blast or projection hazard
H204	Fire or projection hazard
H205	May mass explode in fire
H220	Extremely flammable gas
H221	Flammable gas
H222	Extremely flammable aerosol
H223	Flammable aerosol
H224	Extremely flammable liquid and vapour
H225	Highly flammable liquid and vapour
H226	Flammable liquid and vapour
H227	Combustible liquid
H228	Flammable solid
H229	Pressurized container: may burst if heated
H230	May react explosively even in the absence of air
H231	May react explosively even in the absence of air at elevated pressure and/or temperature
H240	Heating may cause an explosion
H241	Heating may cause a fire or explosion
H242	Heating may cause a fire
H250	Catches fire spontaneously if exposed to air
H251	Self-heating; may catch fire
H252	Self-heating in large quantities; may catch fire
H260	In contact with water releases flammable gases which may ignite spontaneously
H261	In contact with water releases flammable gas
H270	May cause or intensify fire; oxidizer
H271	May cause fire or explosion; strong oxidizer
H272	May intensify fire; oxidizer
H280	Contains gas under pressure; may explode if heated
H281	Contains refrigerated gas; may cause cryogenic burns or injury
H290	May be corrosive to metals
Health hazards
Code	Phrase
H300	Fatal if swallowed
H301	Toxic if swallowed
H302	Harmful if swallowed
H303	May be harmful if swallowed