Journal
BIOPHYSICAL JOURNAL
Volume 90, Issue 2, Pages 681-692Publisher
CELL PRESS
DOI: 10.1529/biophysj.105.061010
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Funding
- NHLBI NIH HHS [R01 HL065631, R29 HL054614, HL054614, R01 HL054614, HL65631] Funding Source: Medline
- NIAID NIH HHS [R01 AI044902, AI 44902, R21 AI044902] Funding Source: Medline
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL065631, R01HL054614, R29HL054614] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI044902, R01AI044902] Funding Source: NIH RePORTER
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In single-molecule mechanics experiments the molecular elasticity is usually measured from the deformation in response to a controlled applied force, e. g., via an atomic force microscope cantilever. We have tested the validity of an alternative method based on a recently developed theory. The concept is to measure the change in thermal fluctuations of the cantilever tip with and without its coupling to a rigid surface via the molecule. The new method was demonstrated by its application to the elasticity measurements of L- and P-selectin complexed with P-selectin glycoprotein ligand-1 or their respective antibodies, which showed values comparable to those measured from the slope of the force-extension curve. L- and P-selectin were found to behave as nearly linear springs capable of sustaining large forces and strains without sudden unfolding. The measured spring constants of similar to 4 and similar to 1 pN/ nm for L- and P-selectin, respectively, suggest that a physiological force of similar to 100 pN would result in an similar to 200% strain for the respective selectins.
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