Self-assembly approach to protein design
- 1 October 1991
- journal article
- Published by IOP Publishing in Nanotechnology
- Vol. 2 (4) , 203-205
- https://doi.org/10.1088/0957-4484/2/4/006
Abstract
A small protein was self-assembled on a template. A metal-binding ligand, 4,4'-dicarboxylic acid-2,2'-bipyridine, was attached to the N-terminus of an oligopeptide with the potential to form an amphiphilic alpha -helix. These bipyridine-modified peptides trimerized to form a three alpha -helix bundle protein in the presence of FE(II). The cumulative binding constant was determined to be >5*1017 M-3, approximately 25 times greater than that of a control compound with no peptide moiety. Aldehyde templates are being developed to assemble unsymmetrical three alpha -helix bundle proteins.Keywords
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