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
Biopolymersjournal_title
Biopolymersauthors
Obataya I,Sakamoto S,Ueno A,Mihara Hdoi
10.1002/1097-0282(200108)59:2<65::AID-BIP1006>3.0.subject
Has Abstractpub_date
2001-08-01 00:00:00pages
65-71issue
2eissn
0006-3525issn
1097-0282pii
10.1002/1097-0282(200108)59:2<65::AID-BIP1006>3.0.journal_volume
59pub_type
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