194033-05-1

Upstream product

• 51-35-4 4R-4-hydroxyproline 
• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 40216-83-9 L-4-hydroxyproline methyl ester hydrochloride 

Downstream Products

• 194033-06-2 (2S,4R)-1-(((benzyloxy)carbonyl)-L-valyl)-4-hydroxypyrrolidine-2-carboxylic acid 
• 727709-23-1 3-(1-benzyloxycarbonylamino-2-methyl-propyl)-6-(tert-butyl-dimethyl-silanyloxy)-6,7-dihydro-5H-pyrrolo[1,2-c]imidazole-1-carboxylic acid pentafluorophenyl ester 
• 727709-17-3 [(2S,4R)-1-((S)-2-Benzyloxycarbonylamino-3-methyl-butyryl)-4-(tert-butyl-dimethyl-silanyloxy)-pyrrolidin-2-yl]-oxo-acetic acid methyl ester 
• 727709-19-5 3-(1-benzyloxycarbonylamino-2-methyl-propyl)-6-(tert-butyl-dimethyl-silanyloxy)-6,7-dihydro-5H-pyrrolo[1,2-c]imidazole-1-carboxylic acid methyl ester 
• 727709-15-1 (2S,4R)-1-((S)-2-Benzyloxycarbonylamino-3-methyl-butyryl)-4-(tert-butyl-dimethyl-silanyloxy)-pyrrolidine-2-carboxylic acid 
• 910469-83-9 [1-[2',5'-bis-O-(tert-butyldimethylsilyl)-β-D-ribofuranosyl]-3-N-[3-N'-[N^α(benzyloxycarbonyl)-valyl-(2S,4R)-4-O-hydroxyprolylamino]propyl]thymine]-3'-spiro-5''-[4''-amino-1'',2''-oxathiole-2'',2''-dioxide] 

Relevant academic research and scientific papers

Domino Process Achieves Site-Selective Peptide Modification with High Optical Purity. Applications to Chain Diversification and Peptide Ligation

The development of peptide libraries by site-selective modification of a few parent peptides would save valuable time and materials in discovery processes but still is a difficult synthetic challenge. Herein, we introduce natural hydroxyproline as a convertible unit for the production of a variety of optically pure amino acids, including expensive N-alkyl amino acids, homoserine lactones, and Agl lactams, and to achieve the mild, efficient, and site-selective modification of peptides. A domino process is used to cleave the customizable Hyp unit under mild, metal-free conditions. Both terminal and internal positions can be modified, and similar customizable units can be differentiated. The resulting products possess two reactive chains which can be manipulated independently. The versatility and scope of this process is highlighted by its application to the ligation of two peptide chains, and the generation of peptides with several chains and peptides with conformational restrictions.

Design and discovery of a novel dipeptidyl-peptidase IV (CD26)-based prodrug approach

Here we describe a novel type of enzyme-based prodrug approach in which a dipeptide moiety is linked to a nonpeptidic therapeutic drug through an amide bond which is specifically cleaved by the dipeptidyl-peptidase IV (DPP IV/CD26) enzyme activity present in plasma and on the surface of certain cells. DPP IV has high substrate selectivity for peptides with a proline (or an alanine) at the penultimate amino acid position at the N-terminus but tolerates a wide range of natural amino acids at the amino terminal end. A variety of dipeptidyl amide prodrugs of anti-HIV TSAO molecules were synthesized and evaluated for their ability to act as substrates for the enzyme. Our data revealed that DPP IV/CD26 can efficiently recognize such prodrugs as substrates, releasing the parent compound. Moreover, it is possible to modify the half-life and the lipophilicity of the prodrugs by changing the nature of the dipeptide. All conjugates have shown marked in vitro antiviral activities irrespective the the nature of the terminal and/or the penultimate amino acid moiety.

Synthesis of a C3-symmetric nanoscale molecular platform based on marine cyclopeptides

Efficient synthesis of a conformationally preorganized, C 3-symmetric molecular platform is reported. The rigid scaffold is based on the structure of marine cyclopeptides and presents three functional groups pointing in the same direction. The bicyclic imidazole building blocks were synthesized in seven steps from trans-4-hydroxy-(S)-proline.