title: Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy.
abstract: The binding force between a liposome and the C2A domain of synaptotagmin I was determined by an atomic force microscopy (AFM). Liposomes were immobilized on the surface of the L1 sensor chip and the C2A domains, which recognize phosphatidylserine, were chemically conjugated onto a gold-coated cantilever tip. The average interaction force between the C2A domain and the liposome was 306 (+/-57) pN while the force between untreated cantilever and the liposome was 58 (+/-16) pN. This work helps understand the physicochemical interactions between proteins and lipid vesicles for the design of high affinity protein probes against the apoptotic cell surface.
authors.affiliation: Department of Mechanical Engineering, Yonsei University, Seoul, South Korea.
authors.forename: Jong-Ho
authors.initials: JH
authors.lastname: Park
authors.forename: Eun-Young
authors.initials: EY
authors.lastname: Kwon
authors.forename: Hyo-Il
authors.initials: HI
authors.lastname: Jung
authors.forename: Dae-Eun
authors.initials: DE
authors.lastname: Kim
mesh_terms: D001665:Binding Sites; D008051:Lipid Bilayers / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D008846:Micromanipulation / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000379:methods*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013314:Stress, Mechanical; D050863:Synaptotagmin I / Q000737:chemistry*
chemical_list: D008051:Lipid Bilayers; D008081:Liposomes; D050863:Synaptotagmin I