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Helix propensities of conformationally restricted amino acids. Non-natural substitutes for helix breaking proline and helix forming alanine

AuthorsAlías, Miriam; Ayuso-Tejedor, Sara; Fernández-Recio, Juan ; Cativiela, Carlos ; Sancho, Javier
Issue Date2010
PublisherRoyal Society of Chemistry (Great Britain)
CitationOrganic and Biomolecular Chemistry 8(4): 788-792 (2010)
AbstractAlpha helices are useful scaffolds to build biologically active peptides. The intrinsic stability of an alpha-helix is a key feature that can be successfully designed, and it is governed by the constituting amino acid residues. Their individual contributions to helix stability are given, according to Lifson–Roig theory, by their w parameters, which are known for all proteinogenic amino acids, but not for non-natural ones. On the other hand, non-natural, conformationally-restricted amino acids can be used to impart biochemical stability to peptides intended for in vivo administration. Efficient design of peptides based on these amino acids requires the previous determination of their w parameters. We begin here this task by determining the w parameters of two restricted analogs of alanine: (α-methyl)alanine and 1-aminocyclopropanecarboxylic acid. According to their w values (α-methyl)alanine is almost as good a helix forming residue as alanine, while 1-aminocyclopropanecarboxylic acid is, similarly to proline, a helix breaker.
Identifiersdoi: 10.1039/B919671D
issn: 1477-0520
e-issn: 1477-0539
Appears in Collections:(ICMA) Artículos
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