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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Cooperative adhesion of ligand-receptor bonds.
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Cooperative adhesion of ligand-receptor bonds.

机译：配体-受体键的合作粘附。

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Cooperative (simultaneous) breakage of multiple adhesive bonds has been proposed as a mechanism for enhanced binding strength between adhesion molecules on apposing cell surfaces. In this report, we used the atomic force microscopy (AFM) to study how changes in binding affinity and separation rate of force-induced ligand-receptor dissociation affect binding cooperativity. The AFM force measurements were carried out using (strept)avidin-functionalized cantilever tips and biotinylated agarose beads under conditions where multiple (strept)avidin-biotin linkages were formed following surface contact. At slow surface separation of the AFM cantilever from the bead's surface, the (strept)avidin-biotin linkages appeared to rupture sequentially. Increasing the separation rate from 210 to 1950 nm/s led to a linear increase in the average rupture force. Moreover, force histograms revealed a quantized force distribution that shifted toward higher values with increasing separation rate. In measurements of streptavidin-iminobiotin adhesion, the force distribution also shifted toward higher values when the buffer was adjusted to a higher pH to raise the binding affinity. Together, these results demonstrate that the cooperativity of ligand-receptor bonds is significantly enhanced by increases in surface separation rate and/or binding affinity.
机译：已经提出了多个粘合键的协同（同时）断裂作为增强对置细胞表面上的粘合分子之间的结合强度的机制。在本报告中，我们使用原子力显微镜（AFM）研究了力诱导的配体-受体解离的结合亲和力和分离率的变化如何影响结合协同作用。在表面接触后形成多个（链）亲和素-生物素键的条件下，使用（链）亲和素-官能化的悬臂末端和生物素化琼脂糖珠进行AFM力测量。在AFM悬臂从珠子表面缓慢分离的情况下，（链）亲和素-生物素键似乎依次破裂。将分离速率从210 nm / s增加到1950 nm / s导致平均断裂力线性增加。此外，力直方图显示了量化的力分布，随着分离率的增加，力分布向更高的值移动。在链霉亲和素-亚氨基生物素粘附力的测量中，当将缓冲液调节至较高的pH以提高结合亲和力时，力分布也向较高的值移动。在一起，这些结果表明，通过增加表面分离速率和/或结合亲和力，配体-受体键的协同作用显着增强。

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