The Roles of Structure, Dynamics and Assembly in the Display of Peptides on Filamentous Bacteriophage

Author:

Opella Stanley J.1

Affiliation:

1. Department of Chemistry and Biochemistry University of California, San Diego La Jolla CA 92035 USA

Abstract

The filamentous bacteriophages are extraordinarily interesting biological organisms in their own right with a fascinating lifecycle that involves the host cell membrane even though they do not possess a membrane themselves. With the ability to accept additional nucleotides they have proven to be among the most useful tools in experimental molecular biology and biotechnology. The structures of the coat proteins of both Class I (fd) and Class II (Pf1) bacteriophages in both their membrane-bound and structural forms in the bacteriophage particles demonstrate fundamental complexity in the structure and dynamics of apparently small helical proteins. The structures or the end points enable a model of the assembly process to be developed. And all of this structural information informs the design and expression of peptides displayed on the surface of bacteriophages, which is one of the principal applications of these systems in biomedical and biotechnological research.

Publisher

The Royal Society of Chemistry

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