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De novo design of orthogonal peptide pairs forming parallel coiled-coil heterodimers

✍ Scribed by Helena Gradišar; Roman Jerala

Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
233 KB
Volume
17
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

We used the principles governing the selectivity and stability of coiled‐coil segments to design and experimentally test a set of four pairs of parallel coiled‐coil‐forming peptides composed of four heptad repeats. The design was based on maximizing the difference in stability between desired pairs and the most stable unwanted combinations using N‐terminal helix initiator residues, favorable combinations of the electrostatic and hydrophobic interaction motifs and negative design motif based on burial of asparagine residues. Experimental analysis of all 36 pair combinations among the eight peptides was performed by circular dichroism (CD). On the basis of CD spectra, each peptide formed a high level of α‐helical structure exclusively in combination with its designed peptide partner which demonstrates the orthogonality of the designed peptide pair set. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.

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## Abstract We introduce a de novo designed peptide model system that enables the systematic study of 1) the role of a membrane environment in coiled‐coil peptide folding, 2) the impact of different domains of an α‐helical coiled‐coil heptad repeat on the interaction with membranes, and 3) the dyna