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Crystal-state conformation of Cα,α-dialkylated peptides containing chiral β-homo-residues

✍ Scribed by Alessandra Romanelli; Isidoro Garella; Valeria Menchise; Rosa Iacovino; Michele Saviano; Daniela Montesarchio; Claude Didierjean; Paola Di Lello; Filomena Rossi; Ettore Benedetti

Publisher
John Wiley and Sons
Year
2001
Tongue
English
Weight
240 KB
Volume
7
Category
Article
ISSN
1075-2617

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📜 SIMILAR VOLUMES

Structural versatility of peptides from
Structural versatility of peptides from Cα,α-dialkylated glycines. I. A conformational energy computation and x-ray diffraction study of homo-peptides from Cα,α-diethylglycine
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Conformational energy computations on a derivative and a homo-dipeptide of C"\*"-diethylglycine were performed. In both cases the Nand C-terminal groups are blocked as acetamido and methylamido moieties, respectively. It was found that the C"3"-diethylglycine residues are conformationally restricted

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## Abstract A single chiral cyclic α,α‐disubstituted amino acid, (3__S__,4__S__)‐1‐amino‐(3,4‐dimethoxy)cyclopentanecarboxylic acid [(__S__,__S__)‐Ac~5~c^dOM^], was placed at the __N__‐terminal or __C__‐terminal positions of achiral α‐aminoisobutyric acid (Aib) peptide segments. The IR and ^1^H NMR

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The molecular structures of four protected isovaline-(Iva-)containing peptides to the pentamer level have been determined by x-ray diffraction. The peptides are t-Boc-Ala-( S ) -1va-Ala-OMe ( t-Boc : tert-butyloxycarbonyl; OMe : methoxy) and its ( R ) -1va diastereomer, and t-Boc-[ Ala-( R ) -Iva],-