Selection of a peptide that adheres to poly(phenylene vinylene) by peptide phage display

CHED 213

Jeannette M. Osterloh, josterlo@calpoly.edu, Chemistry and Biochemistry, California Polytechnic State University, 1 Grand Ave, San Luis Obispo, CA 93407-0402 and Chad E. Immoos, cimmoos@calpoly.edu, Department of Chemistry and Biochemistry, California Polytechnic State University, 1 Grand Ave, San Luis Obispo, CA 93407-0402.
A major obstacle in the development of proteomic arrays and bioelectronic devices is in modulating the interactions of biological compounds with electronic surfaces. Simple and selective methods for protein immobilization are needed and would be useful in the development of protein arrays on electronic transducers. Peptide phage display libraries are being used to isolate novel peptides possessing high binding affinity to materials used in the electronics industry. Phage display panning techniques were used to isolate peptides with high binding affinity to poly(phenylene vinylene). This polymer is a light-emitting conductor currently used in organic light emitting diodes. The phage display peptide libraries utilized in this study were a 12mer and a constrained 10mer containing a fixed disulfide bond. Bacteriophages found to adhere well to the polymer in preliminary binding studies were isolated from these libraries. The sequences and preliminary binding studies of these peptides will be presented.