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Science 14 October 1994:
Vol. 266. no. 5183, pp. 257 - 259
DOI: 10.1126/science.7939660
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Articles

Science, Vol 266, Issue 5183, 257-259
Copyright © 1994 by American Association for the Advancement of Science

articles

Intermolecular forces and energies between ligands and receptors

VT Moy, EL Florin, and HE Gaub

Department of Physics, Technische Universitat Munchen, Garching, Germany.

The recognition mechanisms and dissociation pathways of the avidin-biotin complex and of actin monomers in actin filaments were investigated. The unbinding forces of discrete complexes of avidin or streptavidin with biotin analogs are proportional to the enthalpy change of the complex formation but independent of changes in the free energy. This result indicates that the unbinding process is adiabatic and that entropic changes occur after unbinding. On the basis of the measured forces and binding energies, an effective rupture length of 9.5 +/- 1 angstroms was calculated for all biotin-avidin pairs and approximately 1 to 3 angstroms for the actin monomer-monomer interaction. A model for the correlation among binding forces, intermolecular potential, and molecular function is proposed.


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