It was previously found that a cationic amphiphilic peptide, Ac-(Leu-Ala-Arg-Leu) 3 -NHCH 3 (4 3 ), caused the destabilization of a phospholipid membrane and showed strong antibacterial activity [Lee et al. Biochim. Biophys. Acta 1986; 862: 211 -219]. In order to investigate the effect of changing h
Peptide helices based on α-amino acids
✍ Scribed by Marco Crisma; Fernando Formaggio; Alessandro Moretto; Claudio Toniolo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2006
- Tongue
- English
- Weight
- 286 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Relevant parameters and stereochemical consequences of helices [α‐helix, 3~10~‐helix, β‐bend ribbon spiral, γ‐helix, 2.0~5~‐helix, poly(Pro)~n~ type‐I and ‐II helices, and collagen triple helix] of peptides based on α‐amino acids for use as templates in various branches of chemistry are briefly discussed. © 2005 Wiley Periodicals, Inc. Biopolymers 84: 3–12, 2006
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]
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