摘要
Forced dissociation of selectin-ligand complex is crucial to such biological processes as leukocyte recruitment,thrombosis formation,as well as tumor metastasis<sup>[</sup>1].Although several assays and techniques,e.g.,dynamic force spectroscopy（DFS）,have been applied to probe the complex at single-bond level,the discrepancies in the loading rate dependence of bond rupture force were found in the assays,presumably due to the different pathways in energy landscape and binding kinetics of molecular complexes<sup>[2]</sup>.However,the underlying mechanisms remain unclear.Here an optical trap（OT）assay was used to quantify the bond rupture at r<sub>f</sub>≤20 pN/s
Forced dissociation of selectin-ligand complex is crucial to such biological processes as leukocyte recruitment,thrombosis formation,as well as tumor metastasis[1].Although several assays and techniques,e.g.,dynamic force spectroscopy（DFS）,have been applied to probe the complex at single-bond level,the discrepancies in the loading rate dependence of bond rupture force were found in the assays,presumably due to the different pathways in energy landscape and binding kinetics of molecular complexes[2].However,the underlying mechanisms remain unclear.Here an optical trap（OT）assay was used to quantify the bond rupture at rf≤20 pN/s with
出处
《医用生物力学》
EI
CAS
CSCD
北大核心
2013年第S1期95-96,共2页
Journal of Medical Biomechanics
基金
supported by National Natural Science Foundation of China grants 10902117, 31230027,30730032,and 10332060
