Intermolecular Forces and Energies Between Ligands and Receptors

• Published in: Science (American Association for the Advancement of Science) Vol. 266; no. 5183; pp. 257 - 259
• Main Authors: Moy, Vincent T., Florin, Ernst-Ludwig, Gaub, Hermann E.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 14-10-1994; American Association for the Advancement of Science
• Subjects: Actins; Adhesion; Avidin - chemistry; Avidin - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding energy; Biological and medical sciences; Biotin - analogs & derivatives; Biotin - chemistry; Biotin - metabolism; Chemical bonding; Enthalpy; Free energy; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Interactions. Associations; Intermolecular phenomena; Ligand binding (Biochemistry); Ligands; Microfilaments; Models, Chemical; Molecular biophysics; Monomers; Receptors; Receptors, Drug - chemistry; Streptavidin; Thermodynamics; Contractile protein; Actins; Molecular interaction; Thermodynamic analysis; Biotin; Molecular complex; Avidin
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.7939660

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.