Folding pentapeptides into left and right handed alpha helices

Autor:	David P. Fairlie, Gloria Ruiz-Gómez, Timothy A. Hill, Giovanni Abbenante, Huy N. Hoang
Rok vydání:	2012
Předmět:	chemistry.chemical_classification Circular dichroism Stereochemistry Organic Chemistry Foldamer Peptide Biochemistry Pentapeptide repeat Cyclic peptide Crystallography Protein structure chemistry Drug Discovery Helix Alpha helix
Zdroj:	Tetrahedron. 68:4513-4516
ISSN:	0040-4020
DOI:	10.1016/j.tet.2011.10.108
Popis:	Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::9e07cbc348a89a42d9d4d7420fcae54b https://doi.org/10.1016/j.tet.2011.10.108 Zobrazit plný text záznamu Full Text from ScienceDirect