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 |
|---|---|
| Pages (from-to) | 505-509 |
| Number of pages | 5 |
| Journal | Biotechnology Letters |
| Volume | 28 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 2006 Apr 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
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Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy. / Park, Jong Ho; Kwon, Eun Young; Jung, Hyo Il; Kim, Dae Eun.
In: Biotechnology Letters, Vol. 28, No. 7, 01.04.2006, p. 505-509.Research output: Contribution to journal › Article
TY - JOUR
T1 - Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy
AU - Park, Jong Ho
AU - Kwon, Eun Young
AU - Jung, Hyo Il
AU - Kim, Dae Eun
PY - 2006/4/1
Y1 - 2006/4/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33645887821&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33645887821&partnerID=8YFLogxK
U2 - 10.1007/s10529-006-0010-y
DO - 10.1007/s10529-006-0010-y
M3 - Article
C2 - 16614933
AN - SCOPUS:33645887821
VL - 28
SP - 505
EP - 509
JO - Biotechnology Letters
JF - Biotechnology Letters
SN - 0141-5492
IS - 7
ER -