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

✍ Scribed by Ikuo Obataya; Seiji Sakamoto; Akihiko Ueno; Hisakazu Mihara

Publisher
Wiley (John Wiley & Sons)
Year
2001
Tongue
English
Weight
134 KB
Volume
59
Category
Article
ISSN
0006-3525

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✦ Synopsis

As a model of receptor protein, a series of 3␣-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.

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