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Nmr conformational analysis of cyclopeptidic substrates of serine proteases, containing an ortho or meta aminobenzoic acid residue
Author(s) -
Convert Odile,
Mazaleyrat JeanPaul,
Wakselman Michel,
Morize Isabelle,
ReboudRavaux Michèle
Publication year - 1990
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.360300510
Subject(s) - chemistry , amide , residue (chemistry) , serine , aminobenzoic acid , proteases , hydrolysis , stereochemistry , nuclear magnetic resonance spectroscopy , proton nmr , enzyme , organic chemistry , medicinal chemistry
Cyclopeptides I and II containing an ortho ‐ or meta ‐aminobenzoic acid residue are comparatively analysed by 1 H‐ and 13 C‐nmr. The 1 H‐nmr results, i.e., the temperature coefficients ΔδNH/Δ T , the exchange rates of the amide protons, and nuclear Overhauser effects, suggest a predominant conformation for cyclopeptides I. The meta analogues II present a greater conformational mobility. This observation is related to the greater reactivity of peptides II toward enzymatic hydrolysis, compared to their ortho analogues I.