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.
Original language | English |
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Pages (from-to) | 505-509 |
Number of pages | 5 |
Journal | Biotechnology Letters |
Volume | 28 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2006 Apr |
Bibliographical note
Funding Information:This work was supported by a grant from National Core Research Center (NCRC) for Nanomedical Technology of the Korea Science & Engineering Foundation.
All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology