Design and synthesis of 3alpha-helix peptides forming a cavity for a fluorescent ligand.

Abstract:

:As a model of receptor protein, a series of 3alpha-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.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Obataya I,Sakamoto S,Ueno A,Mihara H

doi

10.1002/1097-0282(200108)59:2<65::AID-BIP1006>3.0.

subject

Has Abstract

pub_date

2001-08-01 00:00:00

pages

65-71

issue

2

eissn

0006-3525

issn

1097-0282

pii

10.1002/1097-0282(200108)59:2<65::AID-BIP1006>3.0.

journal_volume

59

pub_type

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