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Nucleic Acids Research, 1995, Vol. 23, No. 9 1531-1535
© 1995

METHODS

Direct measurement via phage titre of the dissociation constants in solution of fusion phage-substrate complexes

Michael R. Dyson, Volker Germaschewski and Kenneth Murray*

Institute of Cell and Molecular Biology, University of Edinburgh King's Buildings, Mayfield Road, Edinburgh EH9 3JR.UK

*To whom correspondence should be addressed

Received January 5, 1995. Revised March 13, 1995. Accepted March 13, 1995.

Studies of Interactions between filamentous fusion phage particles and protein or nucleic acid molecules have gained Increasing Importance with recent successes of screening techniques based upon random phage display libraries (biopanning). Since a number of different phage are usually obtained by biopanning, it is useful to compare quantitatively the binding affinities of individual phage for the substrate used for selection. A procedure is described for determination of relative dissociation constants (KdRel) between filamentous phage carrying peptide fusions to the coat protein gplll and substrates in solution. This novel method Is based on the measurement of phage titres. Phage selected from a random fusion phage library for binding to a monoclonal antibody or a viral structural protein exhibited KdRel values In the nanomolar and micromolar ranges for their respective substrates, thus validating the method over a wide range of binding affinities.


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