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Anal Biochem. 2011 Oct 1;417(1):149-55. doi: 10.1016/j.ab.2011.06.002. Epub 2011 Jun 12.

Helical peptide arrays for lead identification and interaction site mapping.

Author information

1
Pepscan Therapeutics, 8243 RC Lelystad, The Netherlands. hans.langedijk@crucell.com

Abstract

Libraries composed of linear and cyclic peptides cannot fully represent the higher order structures of most antigenic sites. To map the binding site of ligands or antibodies, a larger part of the three-dimensional space should be sampled. Because parallel synthesis of large arrays of peptides on hydrogels is restricted to relatively small peptides, a simple and robust homodimeric helical system was chosen for antigen presentation. First, it was established in an heterodimeric system that the 26-mer peptide could be synthesized and that the helical coiled-coil peptides interact in the hydrogel in a predictable manner. Next, libraries of homodimeric coiled coils were synthesized into which the epitope was grafted. Using dedicated helical dimeric and trimeric coiled-coil libraries, the epitopes of two anti-HIV-1 gp41 monoclonal antibodies known to interact with helical structures were mapped at high resolution. These mappings precisely reflect existing X-ray data, and the arrays can be applied to lead identification, epitope mapping, and systematic analysis of amino acid contribution to coiled-coil systems.

PMID:
21708118
DOI:
10.1016/j.ab.2011.06.002
[Indexed for MEDLINE]

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