Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy

Esben Thormann; Adam C. Simonsen; Lars K. Nielsen; Ole G. Mouritsen

doi:10.1002/jmr.850

Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy

Esben Thormann, Adam C. Simonsen, Lars K. Nielsen, Ole G. Mouritsen^*

^*Corresponding author af dette arbejde

18 Citationer (Scopus)

Abstract

The atomic force microscope (AFM) and the associated dynamic force spectroscopy technique have been exploited to quantitatively assess the interaction between proteins and their binding to specific ligands and membrane surfaces. In particular, we have studied the specific interaction between lung surfactant protein D and various carbohydrates. In addition, we have used scanning AFM and time-resolved fluorescence microscopy to image the lateral structure of different lipid bilayers and their morphological changes as a function of time. The various systems studied illustrate the potential of modern AFM techniques for application to biomedical research, specifically within immunology and liposome-based drug delivery.

Originalsprog	Engelsk
Tidsskrift	Journal of Molecular Recognition
Vol/bind	20
Udgave nummer	6
Sider (fra-til)	554-560
Antal sider	7
ISSN	0952-3499
DOI	https://doi.org/10.1002/jmr.850
Status	Udgivet - 1 nov. 2007

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title = "Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy",

abstract = "The atomic force microscope (AFM) and the associated dynamic force spectroscopy technique have been exploited to quantitatively assess the interaction between proteins and their binding to specific ligands and membrane surfaces. In particular, we have studied the specific interaction between lung surfactant protein D and various carbohydrates. In addition, we have used scanning AFM and time-resolved fluorescence microscopy to image the lateral structure of different lipid bilayers and their morphological changes as a function of time. The various systems studied illustrate the potential of modern AFM techniques for application to biomedical research, specifically within immunology and liposome-based drug delivery.",

keywords = "Atomic force microscopy, Force spectroscopy, Lateral membrane structure, Ligand-receptor interaction, Phospholipase A, Single molecules, Surfactant protein D",

author = "Esben Thormann and Simonsen, {Adam C.} and Nielsen, {Lars K.} and Mouritsen, {Ole G.}",

year = "2007",

month = nov,

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doi = "10.1002/jmr.850",

language = "English",

volume = "20",

pages = "554--560",

journal = "Journal of Molecular Recognition",

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TY - JOUR

T1 - Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy

AU - Thormann, Esben

AU - Simonsen, Adam C.

AU - Nielsen, Lars K.

AU - Mouritsen, Ole G.

PY - 2007/11/1

Y1 - 2007/11/1

N2 - The atomic force microscope (AFM) and the associated dynamic force spectroscopy technique have been exploited to quantitatively assess the interaction between proteins and their binding to specific ligands and membrane surfaces. In particular, we have studied the specific interaction between lung surfactant protein D and various carbohydrates. In addition, we have used scanning AFM and time-resolved fluorescence microscopy to image the lateral structure of different lipid bilayers and their morphological changes as a function of time. The various systems studied illustrate the potential of modern AFM techniques for application to biomedical research, specifically within immunology and liposome-based drug delivery.

AB - The atomic force microscope (AFM) and the associated dynamic force spectroscopy technique have been exploited to quantitatively assess the interaction between proteins and their binding to specific ligands and membrane surfaces. In particular, we have studied the specific interaction between lung surfactant protein D and various carbohydrates. In addition, we have used scanning AFM and time-resolved fluorescence microscopy to image the lateral structure of different lipid bilayers and their morphological changes as a function of time. The various systems studied illustrate the potential of modern AFM techniques for application to biomedical research, specifically within immunology and liposome-based drug delivery.

KW - Atomic force microscopy

KW - Force spectroscopy

KW - Lateral membrane structure

KW - Ligand-receptor interaction

KW - Phospholipase A

KW - Single molecules

KW - Surfactant protein D

UR - http://www.scopus.com/inward/record.url?scp=38349083220&partnerID=8YFLogxK

U2 - 10.1002/jmr.850

DO - 10.1002/jmr.850

M3 - Journal article

C2 - 17907279

AN - SCOPUS:38349083220

SN - 0952-3499

VL - 20

SP - 554

EP - 560

JO - Journal of Molecular Recognition

JF - Journal of Molecular Recognition

IS - 6

ER -

Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy

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