Abstract
Conformational energy computations on the 1-aminocyclopropane-1-carboxylic acid mono-, di-, and tripeptide amides, (Ac-(Ac 3c) nNHMe ( n=1−3), indicate that this C α,α-dialkylated, cyclic α-amino acid residue is conformally restricted and that type-I(I′) β-bends and distorted 3 10-helices are particularly stable conformations for the di- and tripeptide amides, respectively. The results of the theoretical analysis are in agreement with those obtained in an i.r. absorption and 1H n.m.r. investigation in chloroform solution of A.c. 3c-rich tri- and tetrapeptide esters. A comparisons is also made with the conclusions extracted from our previous work on peptides rich in Aib (α-aminoisobutyric acid), Ac 5c(1-aminocyclopentane-1-carboxylic acid), and Ac 6c (1-aminocyclohexane-1-carboxylic acid).
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