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Lysinonorleucine cross‐link formation in alpha amino heptenoic acid‐substituted peptide derivatives
Author(s) -
Karwoski Gene,
Galione Michael,
Starcher Barry
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170503
Subject(s) - chemistry , tripeptide , lysine , amino acid , sodium borohydride , aldehyde , stereochemistry , peptide , alanine , organic chemistry , biochemistry , catalysis
Studies on the cross‐linking of a tripeptide ( t ‐butyloxycarbonyl‐ L ‐alanyl‐ D , L ‐2‐amino‐6‐heptenoyl‐ L ‐alanine methyl ester) have shown that it is possible to form specific cross‐links in good yields through Schiff base formation of the ε amino group of lysine. The heptenoic acid residue has been ozonized to an aldehyde and condensed with the ε amino of lysine in the compounds alpha‐ t ‐butyloxycarbonyl‐ L ‐alanyl‐ L ‐lysine methyl ester and alpha‐ t ‐butyloxycarbonyl‐ L ‐lysine methyl ester to form the cross‐link, lysinonorleucine. This compound has been stabilized by reduction with sodium borohydride and quantitated on the amino acid analyzer. This technique converts from 60 to 98% of the available aldehyde to lysinonorleucine.