Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy.
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.
Park
Jong-Ho
JH
Department of Mechanical Engineering, Yonsei University, Seoul, South Korea.
Kwon
Eun-Young
EY
Jung
Hyo-Il
HI
Kim
Dae-Eun
DE
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*
D008051:Lipid Bilayers; D008081:Liposomes; D050863:Synaptotagmin I