Premium
Mimicry of dimerization by synthetic peptides designed to target homologous regions of proteins
Author(s) -
Dwyer Donard S.,
Ardizzone Timothy D.
Publication year - 2003
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200390045
Subject(s) - peptide , avidity , biochemistry , peptide sequence , computational biology , biology , gene , chemistry , amino acid , combinatorial chemistry , genetics , antibody
Abstract Rapid progress in sequencing various genomes has highlighted the need for the development of biochemical reagents for the detection of thousands of expressed gene products. The magnitude of this detection problem exceeds current technical capabilities. In an attempt to address this shortcoming, a novel approach has been developed called mimicry of dimerization. Peptide tags have been designed to bind to a specific region of parvalbumin on the basis of amino acid sequence homology with this segment. Multivalent ligands were produced by coupling the synthetic peptides to activated dextran polymers and binding was assessed by chemiluminescence of enhanced avidity reactions using a high density of target protein at the binding surface. Binding of the peptide ligands to parvalbumin was strongest under assay conditions that enriched for native monomeric protein and was affected by pH, temperature and solvent conditions. The results suggest that it should be possible to develop specific reagents for tagging proteins on the basis of sequence and secondary structure information.