108334-64-1

Upstream product

• 63-91-2 L-phenylalanine 
• 58561-04-9 N-tert-butoxycarbonyl-L-valine methyl ester 
• 20902-47-0 N-tert-butoxycarbonyl-L-valyl-L-phenylalanine methyl ester 
• 13734-41-3 t-Boc-L-valine 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 16480-57-2 L-phenylalanine sodium salt 
• 2462-32-0 L-phenylalanine benzyl ester hydrochloride 
• 66447-55-0 ((S)-1-benzylcarbamoyl-2-methyl-propyl)-carbamic acid tert-butyl ester 
• 70669-15-7 benzyl (tert-butoxycarbonyl)-L-valyl-L-phenylalaninate 
• 150114-85-5 N-(tert-butyloxycarbonyl)-L-valyl-L-phenylalanine (methoxyethoxy)ethyl ester 
• 150114-83-3 Boc-Val-Phe-OMoEt 
• 130380-45-9 N-tert-Butyloxycarbonyl-L-valyl-L-phenylalanin-heptylester 
• 3392-12-9 Boc-Val-ONSu 
• 3182-93-2 (L)-phenylalanine ethyl ester hydrochloride 

Downstream Products

• 872983-80-7 2-[2-(2-tert-butoxycarbonylamino-3-methyl-butyrylamino)-3-phenyl-propionylamino]-3-(tert-butyl-dimethyl-silanyloxy)-propionic acid methyl ester 
• 945265-25-8 Boc-Val-Phe-His-OMe 
• 158022-24-3 NH₂-VFM-OMe 
• 1026487-54-6 (S)-2-{(S)-2-[(S)-2-(4-Chloro-2-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1027891-65-1 (S)-2-{(S)-2-[(S)-2-(3-Chloro-4-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1026681-56-0 (S)-2-{(S)-2-[(S)-2-(5-Chloro-2-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1027605-22-6 (S)-2-{(S)-2-[(S)-2-(5-Bromo-2-hydroxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 
• 1026037-79-5 (S)-2-{(S)-2-[(S)-2-(2-Hydroxy-4-methoxy-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionylamino}-4-methylsulfanyl-butyric acid methyl ester 

Relevant academic research and scientific papers

Redox-triggered changes in the self-assembly of a ferrocene-peptide conjugate

Ultrasonication of a ferrocene conjugate of a short amyloid peptide (Aβ18-20) in toluene causes formation of an organogel, which undergoes dramatic structural changes upon oxidation from a nanofibrillar network to spherical micelles. This morphological change is redox-controlled and reversible. the Partner Organisations 2014.

Structure-based design, synthesis, and biological evaluation of peptidomimetic SARS-CoV 3CLpro inhibitors

Structure-based design, synthesis, and biological evaluation of a series of peptidomimetic severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors are described. These inhibitors were designed and synthesized based upon our X-r

Peptide-Chain Elongation Using Unprotected Amino Acids in a Micro-Flow Reactor

Conventional peptide synthesis requires a deprotection step after each amidation step, which decreases synthetic efficiency. Therefore, peptide synthesis using unprotected amino acids is considered an ideal approach. Here, we report peptide chain elongati

A rapid and efficient one-pot method for the reduction of N-protected α-amino acids to chiral α-amino aldehydes using CDI/DIBAL-H

N-Protected amino acids can be easily converted into chiral α-amino aldehydes in a one-pot reaction by activation with CDI followed by reduction with DIBAL-H. This method delivers Boc-, Cbz- and Fmoc-protected amino aldehydes from proteinogenic amino acids in very good isolated yields and complete stereointegrity.

Direct modification of tripeptides using photoinduced decarboxylative radical reactions

In order to explore the applicability of photoinduced electron transfer (PET) promoted decarboxylative reactions to the direct modification of peptides, a study was performed to assess the influence of amino acid side chains on photoreactions of N-terminal protected tripeptides. Photoinduced decarboxylation reactions of tripeptides, which are composed of central amino acids that possess alkyl, phenyl, thioether, hydroxy, and amide containing side chains, in the presence or absence of acrylonitrile and a thiol were found to proceed smoothly to give the corresponding radical addition, H-abstraction, and substitution products. Although photoreactions of tripeptides containing central amino acids with phenol and indole (Tyr and Trp) moieties do not take place efficiently, appropriate protection of these groups enables the substrates to undergo smooth photoinduced decarboxylative reactions.

α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide

The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.

Design, synthesis and SAR studies of tripeptide analogs with the scaffold 3-phenylpropane-1,2-diamine as aminopeptidase N/CD13 inhibitors

Aminopeptidase N (APN), belonged to metalloproteinase, is an essential peptidase involved in the process of tumor invasion and metastasis. A series of tripeptide analogs with the scaffold 3-phenylpropane-1,2-diamine were designed, synthesized and evaluate

Compounds for enzyme inhibition

Peptide-based compounds including heteroatom-containing, three-membered rings efficiently and selectively inhibit specific activities of N-terminal nucleophile (Ntn) hydrolases associated with the proteasome. The peptide-based compounds include an epoxide

Synthesis and evaluation of tripeptidyl α-ketoamides as human rhinovirus 3C protease inhibitors

We describe herein the synthesis and biological evaluation of a series of tripeptidyl α-ketoamides as human rhinovirus (HRV) 3C protease inhibitors. The most potent inhibitor discussed in this manuscript, 4I, exhibited impressive enzyme inhibitory activity as well as antiviral activity against HRV-14.

Phenol-derived CVFM analog inhibitors of Ras farnesyltransferase possessing cellular in vitro activity

A study was performed on structure-activity relationships of a series of phenol-derived, CVFM analogs, inhibitors of Ras Farnesyltransferase (FTase). The effect of various substituents on the phenol ring was examined, while the VFM moiety of the potent inhibitor CVFM was kept constant. The FTase inhibitory activity, reported as IC50 in table I, was influenced by both the chemical properties and the relative position of the substituents on the phenolic ring. The most active compounds in this series contained a chloro or bromine substituent on the phenolic ring. Subsequently we have tested the effects of these FTase inhibitors on the anchorage-dependent growth of two rat epithelial cell lines, FRTL-5 and the same line v-Ha-ras transformed. While most of the compounds were inactive, two showed a growth inhibitory effect: compound 4 was active against normal as well against transformed cells while derivative 13 was active only against transformed cells.