Abstract
Monovalent and multivalent binding and unbinding interactions between peptide-ligands and integrin-receptors on living cell membrane were measured and quantified using an atomic force microscopy (AFM). Initially, we performed single-molecule force spectroscopy measurements with peptide-functionalized AFM probes, targeting specific integrin receptors, and identified and quantified the binding strength as well as receptors’ distribution on the cell membrane. Next, bivalent, trivalent, and multivalent binding interactions were examined and compared by varying the retracing and approaching speed of the AFM probes. Here, we discuss multivalent effects on the binding sensitivity, selectivity, and strength and their dependence on parameters including receptor concentrations of non-cancerous and cancerous cell-lines. This research was supported by the NIGMS/NIH R15GM122063 and 1P20GM109024.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
