Kuo S C, Lauffenburger D A
Department of Chemical Engineering, University of Illinois at Urbana-Champaign 61801.
Biophys J. 1993 Nov;65(5):2191-200. doi: 10.1016/S0006-3495(93)81277-3.
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. (Dembo, M., D.C. Torney, K. Saxman, and D. Hammer. 1988. Proc. R. Soc. Lond. Ser. B 234:55-83).
受体介导的细胞黏附是许多生理和生物技术过程中的核心现象。黏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,但此前尚无针对此问题的实验研究。在此,我们使用径向流体流动腔试验来测量从共价包被有蛋白A的玻璃表面分离共价包被有免疫球蛋白G的聚苯乙烯珠所需的力,以此研究受体/配体黏附强度对键亲和力的依赖性。一系列动物物种来源的免疫球蛋白G使得能够考察三个数量级的蛋白A/免疫球蛋白G结合亲和力。我们针对该模型系统的结果表明,黏附强度随结合亲和力的对数而变化,这与Dembo等人的理论模型预测一致(Dembo, M., D.C. Torney, K. Saxman, and D. Hammer. 1988. Proc. R. Soc. Lond. Ser. B 234:55 - 83)。