23404-17-3Relevant academic research and scientific papers
New system for peptide synthesis using N-acylpyrazoles
Kashima, Choji,Tsuruoka, Shiro,Mizuhara, Saori
, p. 413 - 424 (2007/10/03)
New system of peptide synthesis was described. The extension of one amino acid unit on the peptide chain was constituted from only 2 reaction steps, the conversion from esters to the corresponding N-acylpyrazoles and the subsequent aminolysis with amino esters. This new system was distinctive from the conventional peptide synthesis, which was consisted of 3 steps of the deprotection, the activation and the condensation. Moreover, the key intermediate N-acylpyrazoles exhibited the excellent properties of high sensitivity and separability for the chiral column on HPLC using the UV detector.
ROLE OF AMINO ACID RESIDUES IN CHROMOGENIC SUBSTRATES CLEAVED BY PANCREATIC ELASTASE
Kasafirek, Evzen,Fric, Premysl,Slaby, Jan
, p. 1625 - 1633 (2007/10/02)
Anionic chromogenic substrates, 3-carboxypropionyl tripeptide p-nitroanilides modified with glycine, β-alanine, alanine, leucine, and proline in positions P1, P2, and P3 were synthesized.The substrates were digested with pancreatic elastase and the values of Km, kcat, and kcat/Km were determined.Alanine plays a decisive role in position P1, substrates with glycine or β-alanine in this position are not cleaved.The substitution in P2 is dominant for proline; next follow alanine, leucine, and glycine.The substitution in P3 is the least specific one.
