Abstract
When a system having a series of non-covalently bonded multiple components is pulled to opposite directions from its two ends, sequential and/or simultaneous bond breakages take place. The probability of breakage of individual bonds depends on their intrinsic mechanical properties and on the experimental conditions. We are particularly interested in the pulling mechanics observed when a lectin functional AFM probe was used to pull out the membrane protein, glycophorin A of the red blood cell, together with lipid tether formation. Here our concern is which of the non-covalent interactions, i.e., lectin-glycophorin A or lipid-lipid interactions in the tether is disrupted when the probe is detached from the biomembrane surface. In this paper we conclude that, during the process of lipid tether elongation with a constant tensile force of ∼ 70-80 pN, unbinding of the lectin from glycophorin A takes place with a finite probability in addition to tether breakages that includes complete or incomplete delipidation of glycophorin A. [DOI: 10.1380/ejssnt.2006.273]
