51644-77-0

Upstream product

• 70462-58-7 benzyl (tert-butoxycarbonyl)-L-phenylalanyl-L-prolinate 
• 41324-66-7 H-Pro-OBzl 
• 67729-36-6 Boc-Phe-O-COO-isoBu 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 

Downstream Products

• 82213-83-0 Boc-Phe-Pro-Phe-ProOBzl 
• 1391836-99-9 Boc-Gly-Phe-Gly-Phe-Pro-Trp-OH 
• 1391836-91-1 Boc-Gly-Phe-Gly-Phe-Pro-Trp-OMe 
• 1324010-65-2 C₂₃H₃₃N₃O₆ 
• 1324010-59-4 C₃₁H₃₆N₄O₃ 
• 119351-80-3 (S)-1-{(S)-2-[(S)-2-({(S)-1-[(S)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-3-phenyl-propionyl]-pyrrolidine-2-carbonyl}-amino)-4-methyl-pentanoylamino]-3-phenyl-propionyl}-pyrrolidine-2-carboxylic acid 2,5-dioxo-pyrrolidin-1-yl ester 
• 119351-79-0 (S)-1-{(S)-2-[(S)-2-({(S)-1-[(S)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-3-phenyl-propionyl]-pyrrolidine-2-carbonyl}-amino)-4-methyl-pentanoylamino]-3-phenyl-propionyl}-pyrrolidine-2-carboxylic acid benzyl ester 
• 119351-81-4 (S)-1-{(S)-2-[(S)-2-({(S)-1-[(S)-2-((S)-2-Amino-4-methyl-pentanoylamino)-3-phenyl-propionyl]-pyrrolidine-2-carbonyl}-amino)-4-methyl-pentanoylamino]-3-phenyl-propionyl}-pyrrolidine-2-carboxylic acid 2,5-dioxo-pyrrolidin-1-yl ester 
• 119372-68-8 (S)-1-{(S)-2-[(S)-2-({(S)-1-[(S)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-3-phenyl-propionyl]-pyrrolidine-2-carbonyl}-amino)-4-methyl-pentanoylamino]-3-phenyl-propionyl}-pyrrolidine-2-carboxylic acid 
• 112332-26-0 (5S,8S,10aS,15S,18S,20aS)-5,15-Dibenzyl-8,18-diisobutyl-hexadecahydro-3a,6,9,13a,16,19-hexaaza-dicyclopenta[a,j]cyclooctadecene-4,7,10,14,17,20-hexaone 
• 57225-09-9 Boc-Leu-Phe-Pro-OH 
• 96935-68-1 H-D-Val-Orn(Z)-Leu-Phe-Pro-OH_.HCl 
• 96935-56-7 Boc-D-Val-Orn(Z)-Leu-Phe-Pro-OBzl 
• 96935-58-9 Boc-D-Val-Orn(Z)-Leu-Phe-Pro-OH 

Relevant academic research and scientific papers

Design and synthesis of tryptophan containing peptides as potential analgesic and anti-inflammatory agents

A new series of smaller peptides with tryptophan at C-terminal and varying N-protected amino acids/peptides were designed, synthesized and characterized by analytical and spectroscopic techniques. Analgesic and anti-inflammatory properties of these peptides were carried out in vivo using tail-flick method and carrageenan-induced paw edema method, respectively, at different doses and different time intervals. Most of the peptides synthesized displayed enhanced activity, and particularly tetra and hexapeptides 29-31 were found to be even more potent than the reference standards used. Moreover, some peptides have exhibited promising activity even after 24h of administration, whereas the reference standards were active only up to 3h. Further, the compounds did not present any ulcerogenic liability.

Design, synthesis and evaluation of monovalent Smac mimetics that bind to the BIR2 domain of the anti-apoptotic protein XIAP

We report the systematic rational design and synthesis of new monovalent Smac mimetics that bind preferentially to the BIR2 domain of the anti-apoptotic protein XIAP. Characterization of compounds in vitro (including 9i; ML101) led to the determination of key structural requirements for BIR2 binding affinity. Compounds 9h and 9j sensitized TRAIL-resistant breast cancer cells to apoptotic cell death, highlighting the value of these probe compounds as tools to investigate the biology of XIAP.

Conformational studies of cyclo(L-Phe-L-Pro-Gly-L-Pro)2 by 1H- and 13C-nuclear magnetic resonance spectroscopy, and its enantioface-differentiating ability

Analyses of the 1H- and 13C-nuclear magnetic resonance (1H- and 13C-NMR) spectra of the cyclooctapeptide cyclo (L-Phe-L-Pro-Gly-L-Pro)2 (3) in CDCl3 with the aid of the C-H correlated spectroscopy (C-H COSY) two-dimensional NMR spectrum (Fig. 2) suggested that two kinds of C2-symmetric conformation with all trans and cis-trans-trans-trans forms coexist. When 0.5 eq of CsSCN or 1 eq of D- and L-PheOMe · HCl (D/L ratio = 1/2) was added to a solution of the cyclooctapeptide (3) in CDCl3, the 1H- and 13C-NMR spectra (Fig. 3) suggested the presence of only one C2-symmetric conformation (all trans), resulting from the formation of complexes with CsSCN or D- and L-PheOMe · HCl. The 13C-NMR spectra of the complexes of the cyclooctapeptide (3 or 4) with D- and L-PheOMe · HCl displayed separate resonances for each carbon atom of D-PheOMe · HCl and L-PheOMe · HCl. Furthermore, the ability of 3 to distinguish the D from the L enantiomer, is superior to that of 4 (Table II).

Conformation and Complexation of a Cyclic Dodecapeptide with Alkaline Earth Metal Ions in Acetonitrile

The cyclic dodecapeptide, cyclo(L-Leu-L-Phe-L-Pro)4, was synthesized, and its conformation and complexation with metal ions in acetonitrile were investigated by c.d. and n.m.r. spectroscopy.Cyclo(L-Leu-L-Phe-L-Pro)4 was found to complex selectively with alkaline earth metal ions.The binding constant of the dodecapeptide with Ba2+ was larger than that of the cyclic hexapeptide, cyclo(L-Leu-L-Phe-L-Pro)2.In the free state, the skeletal conformation of the cyclic dodecapeptide ic non-symmetrical.When complexed with Ba2+, the conformation changes to a C4-symmetrical one having all peptide bonds in a trans configuration and four β-turn structures containing transannular hydrogen bonds.Formation of hydrogen bonds on complexation with the cation accounts for the large binding constant of the cyclic dodecapeptide.

Studies on peptide antibiotic 'gratisin'

According to a primary structure proposed for an antibiotic peptide, gratisin, four peptides containing respectively partial sequences, L-Phe-L-Pro-L-Tyr, D-Phe-L-Pro-L-Tyr, L-Phe-L-Pro-D-Tyr, and D-Phe-L-Pro-D-Tyr, were synthesized by a liquid phase meth