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Chemical Structure| 109425-55-0 Chemical Structure| 109425-55-0

Structure of Fmoc-Orn(Boc)-OH
CAS No.: 109425-55-0

Chemical Structure| 109425-55-0

Fmoc-Orn(Boc)-OH

CAS No.: 109425-55-0

4.5 *For Research Use Only !

Cat. No.: A120784 Purity: 97%

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Product Citations

Product Citations

Kotynia, Aleksandra ; Wiatrak, Benita ; Kamysz, Wojciech ; Neubauer, Damian ; Jawien, Paulina ; Marciniak, Aleksandra

Abstract: Antimicrobial peptides are a promising group of compounds used for the treatment of infections. In some cases, metal ions are essential to activate these mols. Examples of metalloantibiotics are, for instance, bleomycin and dermcidin. This study is focused on three new pseudopeptides with potential biol. activity. The coordination behavior of all ligands with Cu(II) and Ni(II) ions has been examined Various anal. methods such as potentiometric titration, UV-Vis and CD spectroscopies, and mass spectrometry were used. All compounds are convenient chelators for metal ion-binding. Two of the ligands tested have histidine residues. Surprisingly, imidazole nitrogen is not involved in the coordination of the metal ion. The N-terminal amino group, Dab side chains, and amide nitrogen atoms of the peptide bonds coordinated Cu(II) and Ni(II) in all the complexes formed. The cytotoxicity of three pseudopeptides and their complexes was evaluated. Moreover, their other model allowed for assessing the attenuation of LPS-induced cytotoxicity and anti-inflammatory activities were also evaluated, the results of which revealed to be very promising.

Keywords: Cu(II) complexes ; LPS-neutralization ; Ni(II) complexes ; anti-inflammatory ; cationic peptides ; potentiometric titration ; spectroscopic methods

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Product Details of [ 109425-55-0 ]

CAS No. :109425-55-0
Formula : C25H30N2O6
M.W : 454.52
SMILES Code : O=C(O)[C@H](CCCNC(OC(C)(C)C)=O)NC(OCC1C2=CC=CC=C2C3=CC=CC=C13)=O
MDL No. :MFCD00065668
InChI Key :JOOIZTMAHNLNHE-NRFANRHFSA-N
Pubchem ID :2756114

Safety of [ 109425-55-0 ]

GHS Pictogram:
Signal Word:Warning
Hazard Statements:H302-H315-H319-H335
Precautionary Statements:P261-P305+P351+P338

Computational Chemistry of [ 109425-55-0 ] Show Less

Physicochemical Properties

Num. heavy atoms 33
Num. arom. heavy atoms 12
Fraction Csp3 0.4
Num. rotatable bonds 13
Num. H-bond acceptors 6.0
Num. H-bond donors 3.0
Molar Refractivity 123.33
TPSA ?

Topological Polar Surface Area: Calculated from
Ertl P. et al. 2000 J. Med. Chem.

113.96 Ų

Lipophilicity

Log Po/w (iLOGP)?

iLOGP: in-house physics-based method implemented from
Daina A et al. 2014 J. Chem. Inf. Model.

3.04
Log Po/w (XLOGP3)?

XLOGP3: Atomistic and knowledge-based method calculated by
XLOGP program, version 3.2.2, courtesy of CCBG, Shanghai Institute of Organic Chemistry

4.1
Log Po/w (WLOGP)?

WLOGP: Atomistic method implemented from
Wildman SA and Crippen GM. 1999 J. Chem. Inf. Model.

4.28
Log Po/w (MLOGP)?

MLOGP: Topological method implemented from
Moriguchi I. et al. 1992 Chem. Pharm. Bull.
Moriguchi I. et al. 1994 Chem. Pharm. Bull.
Lipinski PA. et al. 2001 Adv. Drug. Deliv. Rev.

2.6
Log Po/w (SILICOS-IT)?

SILICOS-IT: Hybrid fragmental/topological method calculated by
FILTER-IT program, version 1.0.2, courtesy of SILICOS-IT, http://www.silicos-it.com

3.39
Consensus Log Po/w?

Consensus Log Po/w: Average of all five predictions

3.48

Water Solubility

Log S (ESOL):?

ESOL: Topological method implemented from
Delaney JS. 2004 J. Chem. Inf. Model.

-4.65
Solubility 0.0101 mg/ml ; 0.0000223 mol/l
Class?

Solubility class: Log S scale
Insoluble < -10 < Poorly < -6 < Moderately < -4 < Soluble < -2 Very < 0 < Highly

Moderately soluble
Log S (Ali)?

Ali: Topological method implemented from
Ali J. et al. 2012 J. Chem. Inf. Model.

-6.2
Solubility 0.000287 mg/ml ; 0.000000633 mol/l
Class?

Solubility class: Log S scale
Insoluble < -10 < Poorly < -6 < Moderately < -4 < Soluble < -2 Very < 0 < Highly

Poorly soluble
Log S (SILICOS-IT)?

SILICOS-IT: Fragmental method calculated by
FILTER-IT program, version 1.0.2, courtesy of SILICOS-IT, http://www.silicos-it.com

-6.56
Solubility 0.000125 mg/ml ; 0.000000275 mol/l
Class?

Solubility class: Log S scale
Insoluble < -10 < Poorly < -6 < Moderately < -4 < Soluble < -2 Very < 0 < Highly

Poorly soluble

Pharmacokinetics

GI absorption?

Gatrointestinal absorption: according to the white of the BOILED-Egg

High
BBB permeant?

BBB permeation: according to the yolk of the BOILED-Egg

No
P-gp substrate?

P-glycoprotein substrate: SVM model built on 1033 molecules (training set)
and tested on 415 molecules (test set)
10-fold CV: ACC=0.72 / AUC=0.77
External: ACC=0.88 / AUC=0.94

Yes
CYP1A2 inhibitor?

Cytochrome P450 1A2 inhibitor: SVM model built on 9145 molecules (training set)
and tested on 3000 molecules (test set)
10-fold CV: ACC=0.83 / AUC=0.90
External: ACC=0.84 / AUC=0.91

No
CYP2C19 inhibitor?

Cytochrome P450 2C19 inhibitor: SVM model built on 9272 molecules (training set)
and tested on 3000 molecules (test set)
10-fold CV: ACC=0.80 / AUC=0.86
External: ACC=0.80 / AUC=0.87

No
CYP2C9 inhibitor?

Cytochrome P450 2C9 inhibitor: SVM model built on 5940 molecules (training set)
and tested on 2075 molecules (test set)
10-fold CV: ACC=0.78 / AUC=0.85
External: ACC=0.71 / AUC=0.81

Yes
CYP2D6 inhibitor?

Cytochrome P450 2D6 inhibitor: SVM model built on 3664 molecules (training set)
and tested on 1068 molecules (test set)
10-fold CV: ACC=0.79 / AUC=0.85
External: ACC=0.81 / AUC=0.87

Yes
CYP3A4 inhibitor?

Cytochrome P450 3A4 inhibitor: SVM model built on 7518 molecules (training set)
and tested on 2579 molecules (test set)
10-fold CV: ACC=0.77 / AUC=0.85
External: ACC=0.78 / AUC=0.86

Yes
Log Kp (skin permeation)?

Skin permeation: QSPR model implemented from
Potts RO and Guy RH. 1992 Pharm. Res.

-6.16 cm/s

Druglikeness

Lipinski?

Lipinski (Pfizer) filter: implemented from
Lipinski CA. et al. 2001 Adv. Drug Deliv. Rev.
MW ≤ 500
MLOGP ≤ 4.15
N or O ≤ 10
NH or OH ≤ 5

0.0
Ghose?

Ghose filter: implemented from
Ghose AK. et al. 1999 J. Comb. Chem.
160 ≤ MW ≤ 480
-0.4 ≤ WLOGP ≤ 5.6
40 ≤ MR ≤ 130
20 ≤ atoms ≤ 70

None
Veber?

Veber (GSK) filter: implemented from
Veber DF. et al. 2002 J. Med. Chem.
Rotatable bonds ≤ 10
TPSA ≤ 140

1.0
Egan?

Egan (Pharmacia) filter: implemented from
Egan WJ. et al. 2000 J. Med. Chem.
WLOGP ≤ 5.88
TPSA ≤ 131.6

0.0
Muegge?

Muegge (Bayer) filter: implemented from
Muegge I. et al. 2001 J. Med. Chem.
200 ≤ MW ≤ 600
-2 ≤ XLOGP ≤ 5
TPSA ≤ 150
Num. rings ≤ 7
Num. carbon > 4
Num. heteroatoms > 1
Num. rotatable bonds ≤ 15
H-bond acc. ≤ 10
H-bond don. ≤ 5

0.0
Bioavailability Score?

Abbott Bioavailability Score: Probability of F > 10% in rat
implemented from
Martin YC. 2005 J. Med. Chem.

0.56

Medicinal Chemistry

PAINS?

Pan Assay Interference Structures: implemented from
Baell JB. & Holloway GA. 2010 J. Med. Chem.

0.0 alert
Brenk?

Structural Alert: implemented from
Brenk R. et al. 2008 ChemMedChem

1.0 alert: heavy_metal
Leadlikeness?

Leadlikeness: implemented from
Teague SJ. 1999 Angew. Chem. Int. Ed.
250 ≤ MW ≤ 350
XLOGP ≤ 3.5
Num. rotatable bonds ≤ 7

No; 1 violation:MW<3.0
Synthetic accessibility?

Synthetic accessibility score: from 1 (very easy) to 10 (very difficult)
based on 1024 fragmental contributions (FP2) modulated by size and complexity penaties,
trained on 12'782'590 molecules and tested on 40 external molecules (r2 = 0.94)

4.41

Application In Synthesis of [ 109425-55-0 ]

* 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 [ 109425-55-0 ]

[ 109425-55-0 ] Synthesis Path-Downstream   1~30

  • 1
  • [ 71989-31-6 ]
  • [ 108-24-7 ]
  • [ 77128-73-5 ]
  • [ 109425-55-0 ]
  • FMOC-D-Cha-OH [ No CAS ]
  • Fmoc-L-Arg(pbf)-Wang resin [ No CAS ]
  • Ac-Phe-Orn-Pro-dCha-(N-Me-Phe)-Arg-OH [ No CAS ]
  • 2
  • 2-chlorotrityl chloride polystyrene resin [ No CAS ]
  • [ 162502-65-0 ]
  • [ 27144-18-9 ]
  • [ 29022-11-5 ]
  • [ 71989-31-6 ]
  • [ 71989-23-6 ]
  • [ 71989-35-0 ]
  • [ 132388-59-1 ]
  • [ 86060-81-3 ]
  • [ 109425-55-0 ]
  • C93H116N11O16PolS2 [ No CAS ]
YieldReaction ConditionsOperation in experiment
Synthesis of the peptide is carried out by a regular stepwise Fmoc SPPS procedure starting from 2-Cl-Trt-chloride resin. The first amino acid (Fmoc-Gly) is loaded on the resin as described in previous examples to obtain a loading of about 0.7 mmol/g of amino acid/resin. After washing of the resin and removal of the Fmoc group by treatment with piperidine/DMF, the second amino acid (Fmoc-Orn(Boc)) is introduced to continue sequence elongation. Fmoc protected amino acids are activated in situ using TBTU/HOBt and subsequently coupled to the resin over about 50 minutes. Diisopropylethylamine or collidine is used during coupling as an organic base. Completion of the coupling is indicated by ninhydrin test. After washing of the resin, the Fmoc protecting group on the alpha-amine is removed with 20% piperidine in DMF for 20 min. These steps are repeated each time with another amino acid according to the peptide sequence. All amino acids used are Fmoc-Nalpha protected. Trifunctional amino acids are side chain protected as follows: Cys(Acm), Thr(tBu), Asn(Trt), and Orn(Boc). Three equivalents of the activated amino acids are used in the coupling reactions. At the end of the synthesis, the peptide-resin is washed with DMF, followed by DCM, and dried under vacuum to obtain dry peptide-resin.
  • 3
  • [ 68858-20-8 ]
  • [ 35661-40-6 ]
  • [ 71989-38-3 ]
  • [ 103213-32-7 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • Fmoc-S-trityl penicillamine [ No CAS ]
  • C60H74N10O10S2 [ No CAS ]
  • 4
  • [ 68858-20-8 ]
  • [ 35661-40-6 ]
  • [ 71989-38-3 ]
  • [ 103213-32-7 ]
  • [ 109425-55-0 ]
  • [ 95753-55-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • Fmoc-S-trityl penicillamine [ No CAS ]
  • C56H71N11O12S2 [ No CAS ]
  • 5
  • [ 353491-47-1 ]
  • [ 67-56-1 ]
  • [ 1730-89-8 ]
  • [ 178924-05-5 ]
  • [ 68858-20-8 ]
  • [ 118904-37-3 ]
  • [ 71989-35-0 ]
  • [ 109425-55-0 ]
  • [ 71989-31-6 ]
  • [ 84624-17-9 ]
  • (4S)-MeHex-D-Val-Thr(tBu)-Val-D-Val-D-Pro-Orn(Boc)-D-aIle-D-Dpr(H-Phe-(Z)Dhb-Val)(Me)-D-aIle-D-Val-OH [ No CAS ]
  • 6
  • [ 353491-47-1 ]
  • [ 1730-89-8 ]
  • [ 178924-05-5 ]
  • [ 68858-20-8 ]
  • [ 118904-37-3 ]
  • [ 71989-35-0 ]
  • [ 109425-55-0 ]
  • [ 71989-31-6 ]
  • [ 84624-17-9 ]
  • (4S)-MeHex-D-Val-Thr(tBu)-Val-D-Val-D-Pro-Orn(Boc)-D-aIle-D-Dpr(H-Phe-(Z)Dhb-Val)-D-aIle-D-Val-OH [ No CAS ]
  • 7
  • [ 1730-89-8 ]
  • [ 178924-05-5 ]
  • [ 68858-20-8 ]
  • [ 118904-37-3 ]
  • [ 71989-35-0 ]
  • [ 109425-55-0 ]
  • [ 71989-31-6 ]
  • [ 84624-17-9 ]
  • (4S)-MeHex-D-Val-Thr(tBu)-Val-D-Val-D-Pro-Orn(Boc)-D-aIle-D-Dpr-D-aIle-D-Val-OH [ No CAS ]
  • 8
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 268734-27-6 ]
  • [ 71989-23-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 1213772-61-2 ]
  • 9
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 268734-27-6 ]
  • [ 71989-23-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • [ 1213773-58-0 ]
  • 10
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 268734-27-6 ]
  • [ 71989-23-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • [ 1213772-94-1 ]
  • 11
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 268734-27-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • [ 1213773-27-3 ]
  • 12
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 71989-23-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • [ 1213772-59-8 ]
  • 13
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 71989-23-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • [ 1213773-56-8 ]
  • 14
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 71989-23-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • [ 1213772-92-9 ]
  • 15
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • [ 1213773-24-0 ]
  • 16
  • [ 143726-85-6 ]
  • [ 109425-55-0 ]
  • [ 1350629-58-1 ]
  • 17
  • [ 71989-31-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 193887-44-4 ]
  • [ 203854-59-5 ]
  • C74H118N12O15 [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: Loading of the HMPB-MBHA-resin: The HMPB-MBHA-resin (theoretical loading=1.2 mmol/g, 2 mmol, 1.67 g) was suspended in 1,2-dichloroethane (10 mL) and concentrated thrice. Then a solution of the first amino acid (5 equiv, 10 mmol), DIC (5 equiv, 10 mmol, 1.54 mL), and DMAP (0.01 equiv, 20 mumol, 3 mg) in dry DCM/DMF (50 mL, 10:1 v/v) was added. The mixture was shaken for 3 h and then drained, washed subsequently with DCM, NMP, DCM, and Et2O. The resin was dried before determination of the loading. The loading procedure was repeated when the loading of the resin was found to be too low.Stepwise elongation: Fmoc-DPhe-HMPB-MBHA-resin (loading of the resin was 0.50 mmol/g, 100 mumol, 200 mg) was submitted to nine cycles of Fmoc solid-phase synthesis with the appropriate commercial amino acid building blocks, or Fmoc-beta2hVal-OH. The side chain of ornithine is protected with a Boc-group. Fmoc removal was effected by treatment with 20% piperidine in NMP for 2×10 min. The resin was subsequently washed with NMP, DCM, MeOH, and finally NMP. Fmoc-AA-OH (2.5 equiv, 250 mumol), HCTU (2.5 equiv, 250 mumol, 103 mg) in NMP was pre-activated for 1 min after the addition of DiPEA (3 equiv, 300 mumol, 53 muL) and then added to the resin. The suspension was shaken for 1.5 h. The resin was washed with NMP, DCM, MeOH, and NMP.Cleavage from the resin: After the final Fmoc deprotection the resin was washed with NMP and DCM and treated with 5 mL 1% TFA in DCM (6×10 min). The filtrates were collected, diluted with toluene (15 mL), and concentrated under reduced pressure. The residue was coevaporated with toluene (2×50 mL).Cyclization: In DMF (80 mL) were dissolved PyBOP (5 equiv, 500 mumol, 260 mg), HOBt (5 equiv, 500 mumol, 77 mg), and DiPEA (15 equiv, 1.5 mmol, 262 muL). The linear decapeptide was dissolved in DMF (5 mL) and added dropwise over 1 h to the reaction mixture. After addition the mixture was stirred for 16 h. The reaction mixture was concentrated in vacuo and the crude mixture was subjected to LH-20 size exclusion chromatography.Boc deprotection: The peptide was dissolved in DCM (2 mL) and TFA (2 mL) was added. The mixture was stirred for 2 h, concentrated, and coevaporated with toluene (2×10 mL). The obtained crude product was applied to preparative HPLC purification. Using gradients of aqueous TFA and acetonitrile the cyclic peptides 1-13 were obtained in the yield range 20-45%.
  • 18
  • [ 71989-31-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 193887-44-4 ]
  • [ 203854-59-5 ]
  • (2R)-2-([(9H-fluoren-9-ylmethoxy)carbonyl]amino}methyl)-3-methylbutanoic acid [ No CAS ]
  • C74H116N12O14 [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: Loading of the HMPB-MBHA-resin: The HMPB-MBHA-resin (theoretical loading=1.2 mmol/g, 2 mmol, 1.67 g) was suspended in 1,2-dichloroethane (10 mL) and concentrated thrice. Then a solution of the first amino acid (5 equiv, 10 mmol), DIC (5 equiv, 10 mmol, 1.54 mL), and DMAP (0.01 equiv, 20 mumol, 3 mg) in dry DCM/DMF (50 mL, 10:1 v/v) was added. The mixture was shaken for 3 h and then drained, washed subsequently with DCM, NMP, DCM, and Et2O. The resin was dried before determination of the loading. The loading procedure was repeated when the loading of the resin was found to be too low.Stepwise elongation: Fmoc-DPhe-HMPB-MBHA-resin (loading of the resin was 0.50 mmol/g, 100 mumol, 200 mg) was submitted to nine cycles of Fmoc solid-phase synthesis with the appropriate commercial amino acid building blocks, or Fmoc-beta2hVal-OH. The side chain of ornithine is protected with a Boc-group. Fmoc removal was effected by treatment with 20% piperidine in NMP for 2×10 min. The resin was subsequently washed with NMP, DCM, MeOH, and finally NMP. Fmoc-AA-OH (2.5 equiv, 250 mumol), HCTU (2.5 equiv, 250 mumol, 103 mg) in NMP was pre-activated for 1 min after the addition of DiPEA (3 equiv, 300 mumol, 53 muL) and then added to the resin. The suspension was shaken for 1.5 h. The resin was washed with NMP, DCM, MeOH, and NMP.Cleavage from the resin: After the final Fmoc deprotection the resin was washed with NMP and DCM and treated with 5 mL 1% TFA in DCM (6×10 min). The filtrates were collected, diluted with toluene (15 mL), and concentrated under reduced pressure. The residue was coevaporated with toluene (2×50 mL).Cyclization: In DMF (80 mL) were dissolved PyBOP (5 equiv, 500 mumol, 260 mg), HOBt (5 equiv, 500 mumol, 77 mg), and DiPEA (15 equiv, 1.5 mmol, 262 muL). The linear decapeptide was dissolved in DMF (5 mL) and added dropwise over 1 h to the reaction mixture. After addition the mixture was stirred for 16 h. The reaction mixture was concentrated in vacuo and the crude mixture was subjected to LH-20 size exclusion chromatography.Boc deprotection: The peptide was dissolved in DCM (2 mL) and TFA (2 mL) was added. The mixture was stirred for 2 h, concentrated, and coevaporated with toluene (2×10 mL). The obtained crude product was applied to preparative HPLC purification. Using gradients of aqueous TFA and acetonitrile the cyclic peptides 1-13 were obtained in the yield range 20-45%.
  • 19
  • Fmoc-β3-(R)-homoleucine [ No CAS ]
  • [ 71989-31-6 ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 203854-59-5 ]
  • C74H118N12O15 [ No CAS ]
  • 20
  • Fmoc-gly-wang resin [ No CAS ]
  • [ 248921-66-6 ]
  • [ 21394-04-7 ]
  • [ 1429504-34-6 ]
  • [ 1429504-44-8 ]
  • [ 71989-14-5 ]
  • [ 35661-38-2 ]
  • [ 109425-55-0 ]
  • (R)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-N-trityl-succinamic acid [ No CAS ]
  • C122H173N17O32 [ No CAS ]
  • 21
  • [ 68858-20-8 ]
  • [ 35661-40-6 ]
  • [ 71989-14-5 ]
  • [ 103213-32-7 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • Fmoc-[β-dimethylcysteine](Trt)-OH [ No CAS ]
  • C55H70N10O11S2 [ No CAS ]
  • 22
  • [ 68858-20-8 ]
  • [ 35661-40-6 ]
  • [ 71989-14-5 ]
  • [ 103213-32-7 ]
  • [ 109425-55-0 ]
  • [ 95753-55-2 ]
  • 1-tert-butoxycarbonyl-N-[(9-fluorenyl)methoxycarbonyl]-D-tryptophan [ No CAS ]
  • Fmoc-[β-dimethylcysteine](Trt)-OH [ No CAS ]
  • C51H67N11O13S2 [ No CAS ]
  • 23
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • [ 35737-15-6 ]
  • [ 135673-97-1 ]
  • Orn-D-Trp-Cha-Nal-D-Phe-His(1-Bzl)-NH<SUB>2</SUB> [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: In a reaction vessel, Fmoc-protected Rink amide MBHA resinwas first swelled in DMF for fifteen min. A solution of 20percent piperidinein DMF was added and mixture shaken mechanically for15 min resulting in the removal of Fmoc group. The required Fmocprotected amino acids and coupling reagent 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) were placed in amino acid vessels sequentially. DMF was added to theamino acid vessel, which was subsequently added (by positivepressure of N2) to the reaction vessel containing the resin, followedby addition of N,N-diisppropylethylamine (DIEA). After 3 h of mechanicalshaking at ambient temperature, the solvent was drainedand the resin washed with DMF (3 x 5 min) followed by methanol(2 x 5 mL). The cycles of deprotection and coupling were repeatedtill the desired peptide chain length was obtained. The resin-boundpeptide was transferred to a round bottom flask, and simultaneousremoval of resin and protective groups was achieved by using acocktail combination of TFA:triisopropylsilane (TIPS):H2O[95:2.5:2.5] for 3 h. The crude peptide was filtered and purified onpreparative HPLC system, and analyzed using solvent system ofCH3CN-H2O-0.1percent CF3COOH in the gradient system: 30 min gradient,30-100percent CH3CN-H2O-0.1percent CF3COOH at 215 nm.
  • 24
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 71989-23-6 ]
  • [ 109425-55-0 ]
  • [ 96402-49-2 ]
  • [ 35737-15-6 ]
  • [ 135673-97-1 ]
  • Orn-D-Trp-Cha-Ile-Nal-His(1-Bzl)-NH<SUB>2</SUB> [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: In a reaction vessel, Fmoc-protected Rink amide MBHA resinwas first swelled in DMF for fifteen min. A solution of 20percent piperidinein DMF was added and mixture shaken mechanically for15 min resulting in the removal of Fmoc group. The required Fmocprotected amino acids and coupling reagent 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) were placed in amino acid vessels sequentially. DMF was added to theamino acid vessel, which was subsequently added (by positivepressure of N2) to the reaction vessel containing the resin, followedby addition of N,N-diisppropylethylamine (DIEA). After 3 h of mechanicalshaking at ambient temperature, the solvent was drainedand the resin washed with DMF (3 x 5 min) followed by methanol(2 x 5 mL). The cycles of deprotection and coupling were repeatedtill the desired peptide chain length was obtained. The resin-boundpeptide was transferred to a round bottom flask, and simultaneousremoval of resin and protective groups was achieved by using acocktail combination of TFA:triisopropylsilane (TIPS):H2O[95:2.5:2.5] for 3 h. The crude peptide was filtered and purified onpreparative HPLC system, and analyzed using solvent system ofCH3CN-H2O-0.1percent CF3COOH in the gradient system: 30 min gradient,30-100percent CH3CN-H2O-0.1percent CF3COOH at 215 nm.
  • 25
  • Fmoc-His(1-Bzl)-OH [ No CAS ]
  • [ 268734-27-6 ]
  • [ 71989-23-6 ]
  • [ 109425-55-0 ]
  • [ 35737-15-6 ]
  • [ 135673-97-1 ]
  • Orn-D-Trp-Cha-Ile-Ala(9-anth)-His(1-Bzl)-NH<SUB>2</SUB> [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: In a reaction vessel, Fmoc-protected Rink amide MBHA resinwas first swelled in DMF for fifteen min. A solution of 20% piperidinein DMF was added and mixture shaken mechanically for15 min resulting in the removal of Fmoc group. The required Fmocprotected amino acids and coupling reagent 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) were placed in amino acid vessels sequentially. DMF was added to theamino acid vessel, which was subsequently added (by positivepressure of N2) to the reaction vessel containing the resin, followedby addition of N,N-diisppropylethylamine (DIEA). After 3 h of mechanicalshaking at ambient temperature, the solvent was drainedand the resin washed with DMF (3 x 5 min) followed by methanol(2 x 5 mL). The cycles of deprotection and coupling were repeatedtill the desired peptide chain length was obtained. The resin-boundpeptide was transferred to a round bottom flask, and simultaneousremoval of resin and protective groups was achieved by using acocktail combination of TFA:triisopropylsilane (TIPS):H2O[95:2.5:2.5] for 3 h. The crude peptide was filtered and purified onpreparative HPLC system, and analyzed using solvent system ofCH3CN-H2O-0.1% CF3COOH in the gradient system: 30 min gradient,30-100% CH3CN-H2O-0.1% CF3COOH at 215 nm.
  • 26
  • [ 86123-10-6 ]
  • [ 109425-55-0 ]
  • [ 35737-15-6 ]
  • [ 161420-87-7 ]
  • (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(p-tolyl)propanoic acid [ No CAS ]
  • Orn-D-Trp-D-Phe-Phe(4-Me)-D-Phe-Dab-NH<SUB>2</SUB> [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: In a reaction vessel, Fmoc-protected Rink amide MBHA resinwas first swelled in DMF for fifteen min. A solution of 20% piperidinein DMF was added and mixture shaken mechanically for15 min resulting in the removal of Fmoc group. The required Fmocprotected amino acids and coupling reagent 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate (TBTU) were placed in amino acid vessels sequentially. DMF was added to theamino acid vessel, which was subsequently added (by positivepressure of N2) to the reaction vessel containing the resin, followedby addition of N,N-diisppropylethylamine (DIEA). After 3 h of mechanicalshaking at ambient temperature, the solvent was drainedand the resin washed with DMF (3 x 5 min) followed by methanol(2 x 5 mL). The cycles of deprotection and coupling were repeatedtill the desired peptide chain length was obtained. The resin-boundpeptide was transferred to a round bottom flask, and simultaneousremoval of resin and protective groups was achieved by using acocktail combination of TFA:triisopropylsilane (TIPS):H2O[95:2.5:2.5] for 3 h. The crude peptide was filtered and purified onpreparative HPLC system, and analyzed using solvent system ofCH3CN-H2O-0.1% CF3COOH in the gradient system: 30 min gradient,30-100% CH3CN-H2O-0.1% CF3COOH at 215 nm.
  • 27
  • [ 18523-48-3 ]
  • Fmoc-Ile-Wang resin [ No CAS ]
  • [ 29022-11-5 ]
  • [ 71989-31-6 ]
  • [ 71989-33-8 ]
  • [ 77128-73-5 ]
  • [ 109425-55-0 ]
  • (3aS,7aS)-octahydroindole-2-carboxylic acid [ No CAS ]
  • N-[(9-fluorenyl)methoxycarbonyl]-3-(2-naphthyl)-D-alanine [ No CAS ]
  • Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
  • C68H99N17O15 [ No CAS ]
  • 28
  • Fmoc-Ile-Wang resin [ No CAS ]
  • [ 29022-11-5 ]
  • [ 71989-31-6 ]
  • [ 71989-33-8 ]
  • [ 77128-73-5 ]
  • [ 109425-55-0 ]
  • (3aS,7aS)-octahydroindole-2-carboxylic acid [ No CAS ]
  • N-[(9-fluorenyl)methoxycarbonyl]-3-(2-naphthyl)-D-alanine [ No CAS ]
  • Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
  • [ 137076-54-1 ]
  • C82H124N18O21 [ No CAS ]
  • 29
  • [ 3235-69-6 ]
  • [ 159610-93-2 ]
  • C26H19N2O5Pol [ No CAS ]
  • [ 109425-55-0 ]
  • [ 132684-59-4 ]
  • Mor-Hfe-Ser(Me)-Orn-ACC [ No CAS ]
  • 30
  • [ 3235-69-6 ]
  • [ 159610-93-2 ]
  • [ 35661-60-0 ]
  • C26H19N2O5Pol [ No CAS ]
  • [ 109425-55-0 ]
  • Mor-Orn-Ser(Me)-Leu-ACC [ No CAS ]
 

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