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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy. / Thormann, Esben; Simonsen, Adam C.; Nielsen, Lars K.; Mouritsen, Ole G.

In: Journal of Molecular Recognition, Vol. 20, No. 6, 2007, p. 554-560.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Thormann, E, Simonsen, AC, Nielsen, LK & Mouritsen, OG 2007, 'Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy', Journal of Molecular Recognition, vol. 20, no. 6, pp. 554-560. https://doi.org/10.1002/jmr.850

APA

Thormann, E., Simonsen, A. C., Nielsen, L. K., & Mouritsen, O. G. (2007). Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy. Journal of Molecular Recognition, 20(6), 554-560. https://doi.org/10.1002/jmr.850

Vancouver

Thormann E, Simonsen AC, Nielsen LK, Mouritsen OG. Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy. Journal of Molecular Recognition. 2007;20(6):554-560. https://doi.org/10.1002/jmr.850

Author

Thormann, Esben ; Simonsen, Adam C. ; Nielsen, Lars K. ; Mouritsen, Ole G. / Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy. In: Journal of Molecular Recognition. 2007 ; Vol. 20, No. 6. pp. 554-560.

Bibtex

@article{c62f4866331344d890269003f7915653,
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",
doi = "10.1002/jmr.850",
language = "English",
volume = "20",
pages = "554--560",
journal = "Journal of Molecular Recognition",
issn = "0952-3499",
publisher = "Wiley",
number = "6",
note = "AFM BioMed 2007, Atomic force microscopy in life sciences and medicine ; Conference date: 19-04-2007 Through 21-04-2007",

}

RIS

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

Y1 - 2007

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

U2 - 10.1002/jmr.850

DO - 10.1002/jmr.850

M3 - Journal article

C2 - 17907279

AN - SCOPUS:38349083220

VL - 20

SP - 554

EP - 560

JO - Journal of Molecular Recognition

JF - Journal of Molecular Recognition

SN - 0952-3499

IS - 6

T2 - AFM BioMed 2007, Atomic force microscopy in life sciences and medicine

Y2 - 19 April 2007 through 21 April 2007

ER -

ID: 230977523