Conformational disturbance induced by AzPro/Pro substitution in peptides View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-12

AUTHORS

Alain Bac, Katell Rivoal, Manh Thong Cung, Guy Boussard, Michel Marraud, Benoît Soudan, Daniel Tetaert, Pierre Degand

ABSTRACT

Consequences inherent to the substitution ofaza-proline (AzPro) for proline in the octapeptideTTSAPTTS, representative of the tandem repeat motifpresent in the peptide backbone of MUC5AC mucin, wereanalysed in terms of conformational perturbation andO-glycosylation aptitude. In DMSO solution, weobserved the same tendency previously noted inAzPro-tripeptide models, i.e. AzPro preventsβ-turn formation in which it would occupy thei+1 position, and therefore behaves quite oppositeto Pro, whereas both AzPro and Pro can support aβ-turn in the i+2 position with a cisdisposition of the preceding tertiary amide function.The former structural modifications do not preventO-glycosylation to take place at the same specificsite, but it occurs at a reduced rate. More... »

PAGES

251-258

References to SciGraph publications

  • 1995-11. Synthesis and conformational analysis of AzAsx-containing oligopeptides in INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1023/a:1008868014779

    DOI

    http://dx.doi.org/10.1023/a:1008868014779

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1042795579


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