Nonstereogenic α-aminoisobutyryl-glycyl dipeptidyl unit nucleates type I′ β-turn in linear peptides in aqueous solution
| Autor: | Fernando Porcelli, George Barany, Gianluigi Veglia, Robert P. Hammer, Larry R. Masterson, Marcus A. Etienne |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Aminoisobutyric Acids Stereochemistry Glycine Biophysics Sequence (biology) Backbone conformation Biochemistry Biomaterials Nuclear Magnetic Resonance Biomolecular Peptide sequence chemistry.chemical_classification Aqueous solution Chemistry Circular Dichroism Organic Chemistry Temperature Stereoisomerism General Medicine Amides Amino acid Solutions NMR spectra database Protein folding Protons Peptides Unit (ring theory) |
| Zdroj: | Biopolymers. 88:746-753 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.20738 |
| Popis: | The use of alpha,alpha-disubstituted amino acids represents a valuable strategy to exercise conformational control in peptides. Incorporation of the nonstereogenic alpha-aminoisobutyryl-glycyl (Aib-Gly) dipeptidyl sequence into i+1 and i+2 positions of an acyclic peptide sequence, originally designed and investigated by Gellman and coworkers, [H-Arg-Tyr-Val-Glu-Val-Yyy-Xxx-Orn-Lys-Ile-Leu-Gln-NH2] nucleates a stable [2:4] left-handed type I' beta-turn in water. NMR spectra show that this newly designed beta-hairpin does not aggregate in water up to a concentration of approximately 1 mM, and that its backbone conformation is superimposable on corresponding hairpins containing the DPro-Gly (literature) and Aib-DAla (this work) sequences. The Aib-Gly turn-inducer sequence eliminates complications because of cis-trans isomerization of Zzz-Pro bonds, and constitutes an attractive alternative to the proteogenic Asn-Gly and nonproteogenic DPro-Gly motifs previously suggested as turn-inducer sequences. These design principles could be exploited to prepare water-soluble beta-hairpin peptides with robust structures and novel function. |
| Databáze: | OpenAIRE |
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