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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/52780
Title: Helix propensities of conformationally restricted amino acids. Non-natural substitutes for helix breaking proline and helix forming alanine
Authors: Alías, Miriam; Ayuso-Tejedor, Sara; Fernández-Recio, Juan; Cativiela, Carlos; Sancho, Javier
Issue Date: 2010
Publisher: Royal Society of Chemistry (Great Britain)
Citation: Organic and Biomolecular Chemistry 8(4): 788-792 (2010)
Abstract: Alpha 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.
URI: http://hdl.handle.net/10261/52780
DOI: 10.1039/B919671D
Identifiers: doi: 10.1039/B919671D
issn: 1477-0520
e-issn: 1477-0539
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