57225-09-9

Upstream product

• 95716-19-1 N-(tert-butyloxycarbonyl)-L-leucyl-L-phenylalanyl-L-proline benzyl ester 
• 41324-66-7 H-Pro-OBzl 
• 70462-58-7 benzyl (tert-butoxycarbonyl)-L-phenylalanyl-L-prolinate 
• 51644-77-0 H-Phe-Pro-OBzl 
• 38017-89-9 t-butyloxycarbonyl-L-phenylalanyl-L-proline methyl ester 
• 69936-03-4 (1S)-methyl 2-[(S)-2-amino-3-phenylpropanoyl]cyclopentanecarboxylate 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 159174-83-1 Boc-Leu-Phe-Pro-OMe 

Downstream Products

• 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 
• 119351-81-4 (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 
• 159174-93-3 Boc-Leu-Phe-Pro-Tyr(Bzl)-Val-Pro-OH 
• 159174-88-6 Boc-Leu-Phe-Pro-Tyr(Bzl)-Val-Pro-OMe 
• 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 

Relevant academic research and scientific papers

Isolation and structural determination of phepropeptins A, B, C, and D, new proteasome inhibitors, produced by Streptomyces sp.

We have isolated four related compounds named phepropeptins A, B, C, and D, as inhibitors of proteasome proposed to regulate many cellular functions. From an NMR analysis, the phepropeptins appeared as cyclic hexapeptides, differing in the two residues of the constituent amino acids from one another, with four conserved amino acid moieties. Based on an amino acid analysis, we synthesized two possible cyclic peptides to phepropeptin B that differ in the configurations. A comparison of the properties between the natural and synthesized compounds revealed that the structure of phepropeptin B was cyclo(-L-Leu-D-Phe-L-Pro-L-Phe-D-Leu-L-Val-). The phepropeptins showed inhibition to the proteasomal chymotrypsin-like activity but not to α-chymotrypsin.

A Cyclic Analogue of Hexapeptide Tyr-Val-Pro-Leu-Phe-Pro, A Peptide Immunostimulant

A cyclic analogue of the peptide immunoeffector, hexapeptide Tyr-Val-Pro-Leu-Phe-Pro, was synthesized by different methods in solution.A comparison of the BOP reagent with the classical p-nitrophenyl ester method for the cyclization reaction shows that in

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.