Premium
Design and synthesis of 3α‐helix peptides forming a cavity for a fluorescent ligand
Author(s) -
Obataya Ikuo,
Sakamoto Seiji,
Ueno Akihiko,
Mihara Hisakazu
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(200108)59:2<65::aid-bip1006>3.0.co;2-v
Subject(s) - chemistry , peptide , helix bundle , helix (gastropod) , fluorescence , ligand (biochemistry) , amino acid residue , peptide sequence , biophysics , sequence (biology) , hydrophobic effect , binding site , receptor , stereochemistry , protein structure , combinatorial chemistry , biochemistry , ecology , physics , quantum mechanics , snail , gene , biology
As a model of receptor protein, a series of 3α‐helix bundle peptides constructed on a template peptide were designed so as to possess a hydrophobic cavity. The size of cavity was modulated by simple replacements of Leu residues to Ala residues in the hydrophobic core. Binding abilities to 8‐anilino‐1‐naphthalenesulfonic acid (ANS) were estimated by the increase of fluorescence intensity. The peptide having three or four Ala residues in the hydrophobic core remarkably increased the binding ability for ANS, though the peptide having two Ala residues gave an inefficient cavity for ANS. The peptide having six Ala residues decreased the binding ability due to crucial destabilization of the helix bundle structure. This scaffold can be utilized to a receptor model, while further tuning of the sequence is necessary. © 2001 John Wiley & Sons, Inc. Biopolymers 59: 65–71, 2001