ISSN:
1573-3904
Keywords:
Aza-peptide
;
Aza-proline
;
Beta-turn
;
O-glycosylation
;
Mucin
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008868014779
Permalink
