4864-80-6

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 141-43-5 ethanolamine 
• 60379-01-3 N-(benzyloxycarbonyl)-L-phenylalanine benzyl ester 
• 501-53-1 benzyl chloroformate 
• 771-61-9 2,3,4,5,6-pentafluorophenol 
• 3338-35-0 cyanomethyl ((benzyloxy)carbonyl)phenylalaninate 
• 3588-57-6 Z-DL-Phe-OH 
• 150-30-1 Phenylalanine 
• 6372-14-1 N-((benzyloxy)carbonyl)-L-phenylalaninol 
• 59830-60-3 benzyl (1S)-(1-formyl-2-phenylethyl)carbamate 
• 3182-95-4 L-Phenylalaninol 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 

Downstream Products

• 13122-99-1 (S)-2-(2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)acetic acid 
• 179820-07-6 N-Benzyloxycarbonyl-L-phenylalanine-N-2-(2-methoxy-ethoxymethoxy)ethylamide 
• 1314881-17-8 BrH*C₂₈H₃₀N₂O₄ 
• 1314881-18-9 Cbz-Glu(OMe)-Phaol(Fmoc)-Ac 
• 1314881-19-0 C₃₄H₄₈N₂O₉ 
• 1314881-20-3 2-[(2-{[(benzyloxy)carbonyl]amino}-3-phenylpropyl)(tertbutoxycarbonyl)amino]ethyl tert-butyl carbonate 
• 85304-32-1 N-(2S-2-benzyloxycarbonylamino-3-phenylpropyl)-N-(9-fluorenylmethyloxy-carbonyl)aminoethanol 
• 773806-27-2 2-Amino-N-(2-chloro-ethyl)-3-phenyl-propionamide 
• 94304-12-8 DL-N-Carbobenzoxy-phenylalanin-(2-chlorethyl)-amid 
• 22839-77-6 N-Benzyloxycarbonyl-β-O-benzyl-Asp-Phe-aethanolamid 
• 22849-04-3 Asp-Phe-Aethanolamid 
• 116506-70-8 N-benzyloxycarbonyl-L-phenylalanylglycylaminoethanol 
• 37700-64-4 (5S)-5-benzyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazadodecan-12-oic acid 
• 115788-70-0 Tyr-D-Arg-Phe-NH(CH₂)2OH 

Relevant academic research and scientific papers

A comparative study of warheads for design of cysteine protease inhibitors

The effects on potency of cruzain inhibition of replacing a nitrile group with alternative warheads were explored. The oxime was almost an order of magnitude more potent than the corresponding nitrile and has the potential to provide access to the prime side of the catalytic site. Dipeptide aldehydes and azadipeptide nitriles were found to be two orders of magnitude more potent cruzain inhibitors than the corresponding dipeptide nitriles although potency differences were modulated by substitution at P1 and P3. Replacement of the α methylene of a dipeptide aldehyde with cyclopropane led to a loss of potency of almost three orders of magnitude. The vinyl esters and amides that were characterized as reversible inhibitors were less potent than the corresponding nitrile by between one and two orders of magnitude.

Synthesis of the orthogonally protected amino alcohol Phaol and analogs

The development of a multigram synthesis of the orthogonally protected amino acid-derived Phaol [2-{[(2S)-2-amino-3-phenylpropyl]amino}ethanol] is described. The goal of this work is to synthesize an orthogonally protected Phaol in a multigram scale up to

Development of α-keto-based inhibitors of cruzain, a cysteine protease implicated in Chagas disease

Trypanosoma cruzi, a protozoan parasite, is the causative agent of Chagas disease, a major cause of cardiovascular disease in many Latin American countries. There is an urgent need to develop an improved therapy due to the toxicity of existing drugs and emerging drug resistance. Cruzain, the primary cysteine protease of T. cruzi, is essential for the survival of the parasite in host cells and therefore is an important target for the development of inhibitors as potential therapeutics. A novel series of α-ketoamide-, α-ketoacid-, α-ketoester-, and aldehyde-based inhibitors of cruzain has been developed. The inhibitors were identified by screening protease targeted small molecule libraries and systematically optimizing the P1, P2, P3, and P1′ residues using specific structure-guided methods. A total of 20 compounds displayed picomolar potency in in vitro assays and three inhibitors representing different α-keto-based inhibitor scaffolds demonstrated anti-trypanosomal activity in cell culture. A 2.3 A crystallographic structure of cruzain bound with one of the α-ketoester analogs is also reported. The structure and kinetic assay data illustrate the covalent binding, reversible inhibition mechanism of the inhibitor. Information on the compounds reported here will be useful in the development of new lead compounds as potential therapeutic agents for the treatment of Chagas disease and as biological probes to study the role that cruzain plays in the pathology. This study also demonstrates the validity of structure-guided approaches to focused library design and lead compound optimization.

Nickel complexes from α-amino amides as efficient catalysts for the enantioselective Et2Zn addition to benzaldehyde

Ni2+ complexes derived from simple α-amino amides catalyze very efficiently the addition of Et2Zn to benzaldehyde, giving (S)-1-phenylethanol as the major isomer in most cases (94% yield, 97% ee for R=Bn). The nature of the substituent on the amide nitrogen atom seems to play a key role in determining the asymmetric induction observed.

METALLOPROTEINASE INHIBITORS

Compounds of general formula (I), principally characterized in that R4 is a polyether group, are water soluble matrix metalloproteinase inhibitors. STR1

Design and synthesis of a targeted set of aromatic amino acid derivatives for identification of new lead compounds.

A targeted set of 256 aromatic α-amino acid derivatives is described to provide new lead compounds for biological screening. The utility is exemplified by identification of ligands for the human neuromedin B (hNMB) receptor, such as compound 3 (Ki hNMB 37nM).

Exploitation of subtilisin BPN' as catalyst for the synthesis of peptides containing noncoded amino acids, peptide mimetics and peptide conjugates

The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts nume

STRUCTURAL ELUCIDATION OF AIBELLIN, A NEW PEPTIDE ANTIBIOTIC WITH EFFICIENCY ENHANCING ACTIVITY ON RUMEN FERMENTATION

A new peptide antibiotic, aibellin, that had the afficiency enhancing activity on rumen fermentation, was isolated from the culture broth of the fungus, Verticimonosporium ellipticum D1528, and its primary structure was elucidated from spectrometric analysis and chemical degradation.Aibellin is a 20-residue peptaibol, and it has a unique structural feature in the novel C-terminal amino alcohol.Moreover, aibellin is the first peptaibol that possesses two acidic amino acids in the C-terminal region and a Phe residue in the middle of the sequence.

Amino alcohols as C-Terminal Protecting Groups in Peptide Synthesis

The synthesis of peptides using amino alcohols as C-terminal protecting groups is described.C-Terminal protection of amino acid could be accomplished by reduction of the terminal carboxyl group to a hydroxymethyl group, and regeneration of the carboxyl group could be achieved by Jones' oxidation.This method was applied to the formation of di- and tripeptides.