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Pseudopeptides and β folding: X-ray structures compared with structures in solution

✍ Scribed by André Aubry; Michel Marraud

Book ID
102762411
Publisher
Wiley (John Wiley & Sons)
Year
1989
Tongue
English
Weight
773 KB
Volume
28
Category
Article
ISSN
0006-3525

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✦ Synopsis

In order to restrain the flexibility of the peptide molecules and reduce their biodegradation, modifications of the main chain me now introduced in pseudopeptide analogues. Surprisingly, there is very little data on the conformational properties of these derivatives. We have examined pseudopeptide analogues of RCO-X-Y-NHR model dipeptides in the depsi, N-methylated, reduced, retrq a,P-dehydro, amino acid, and hydrazino wries, in the solid state by x-ray diffraction, and in solution by ir and 'H-nmr spectrascopy. This study provides us with accurate dimensions of the peptide surrogates, and gives some information on the conformational tendencies induced by these substitutions, with reference to those of the related dipeptide sequences.

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