RELATIONSHIP BETWEEN RECEPTOR-LIGAND BINDING-AFFINITY AND ADHESION STRENGTH

RELATIONSHIP BETWEEN RECEPTOR-LIGAND BINDING-AFFINITY AND ADHESION STRENGTH
复制标题

DOI:
10.1016/s0006-3495(93)81277-3
复制
发表时间:
1993-11-01
影响因子:
3.4
通讯作者:
LAUFFENBURGER, DA
LAUFFENBURGER, DA
中科院分区:
生物学3区
文献类型:
--
作者:
KUO, SC;LAUFFENBURGER, DA

文献摘要

被引文献

相似文献

受体介导的细胞粘附是许多生理和生物技术过程中的中心现象。粘附的机械强度通常被认为与受体/配体键的化学亲和力有关,但以前没有针对这个问题的实验研究。在这里,我们调查的依赖性受体/配体的粘附强度对键亲和力使用径向流体流动室测定,以测量所需的力,以脱离共价包被有免疫球蛋白G从玻璃表面共价包被有蛋白A的聚苯乙烯珠。免疫球蛋白G的一系列动物种属来源允许检查三十年的蛋白A/免疫球蛋白G结合亲和力。我们的研究结果表明,该模型系统的粘附强度随结合亲和力的对数而变化,与Dembo等人的理论模型预测一致。
Receptor-mediated cell adhesion is a central phenomenon in many physiological and biotechnological processes. Mechanical strength of adhesion is generally presumed to be related to chemical affinity of receptor/ligand bonds, but no experimental study has been previously directed toward this issue. Here we investigate the dependence of receptor/ligand adhesion strength on bond affinity using a radial fluid flow chamber assay to measure the force needed to detach polystyrene beads covalently coated with immunoglobulin G from glass surfaces covalently coated with protein A. A spectrum of animal species sources for immunoglobulin G permits examination of three decades of protein A/immunoglobulin G binding affinity. Our results for this model system demonstrate that adhesion strength varies with the logarithm of the binding affinity, consistent with a prediction from the theoretical model by Dembo et al.