Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy

Jong Ho Park; Eun Young Kwon; Hyo Il Jung; Dae Eun Kim

doi:10.1007/s10529-006-0010-y

Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy

Jong Ho Park, Eun Young Kwon, Hyo Il Jung, Dae Eun Kim

Department of Mechanical Engineering

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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	https://doi.org/10.1007/s10529-006-0010-y
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

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10.1007/s10529-006-0010-y

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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.",

author = "Park, {Jong Ho} and Kwon, {Eun Young} and Jung, {Hyo Il} and Kim, {Dae Eun}",

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.",

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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

N1 - Funding Information: This work was supported by a grant from National Core Research Center (NCRC) for Nanomedical Technology of the Korea Science & Engineering Foundation.

PY - 2006/4

Y1 - 2006/4

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.

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Direct force measurement of the interaction between liposome and the C2A domain of synaptotagmin I using atomic force microscopy

Abstract

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