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Molecular Recognition Force Microscopy: From Molecular Bonds to Complex Energy Landscapes

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Nanotribology and Nanomechanics I

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Abstract

Atomic force microscopy (AFM), atomic force microscopy (AFM) developed in the late 1980s to explore atomic details on hard material surfaces, has evolved into a method capable of imaging fine structural details of biological samples. Its particular advantage in biology is that measurements can be carried out in aqueous and physiological environments, which opens the possibility to study the dynamics of biological processes in vivo. The additional potential of the AFM to measure ultralow forces at high lateral resolution has paved the way for measuring inter- and intramolecular forces of biomolecules on the single-molecule level. Molecular recognition studies using AFM open the possibility to detect specific ligand–receptor interaction forces and to observe molecular recognition of a single ligand–receptor pair. Applications include biotin–avidin, antibody–antigen, nitrilotriacetate (NTA)–hexahistidine 6, and cellular proteins, either isolated or in cell membranes.

The general strategy is to bind ligands to AFM tips and receptors to probe surfaces (or vice versa). In a force–distance cycle, the tip is first approached towards the surface, whereupon a single receptor–ligand complex is formed due to the specific ligand receptor recognition. During subsequent tip–surface retraction a temporarily increasing force is exerted on the ligand–receptor connection, thus reducing its lifetime until the interaction bond breaks at a critical (unbinding) force. Such experiments allow for estimation of affinity, rate constants, and structural data of the binding pocket. Comparing them with values obtained from ensemble-average techniques and binding energies is of particular interest. The dependences of unbinding force on the rate of load increase exerted on the receptor–ligand bond receptor–ligand bond reveal details of the molecular dynamics of the recognition process and energy landscapes. Similar experimental strategies have also been used for studying intramolecular force properties of polymers and unfolding–refolding kinetics of filamentous proteins. Recognition recognition imaging imaging, developed by combing dynamic force microscopy force microscopy with force spectroscopy, allows for localization of receptor sites on surfaces with nanometer positional accuracy.

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Abbreviations

AFM:

atomic force microscope

AFM:

atomic force microscopy

BFP:

biomembrane force probe

BSA:

bovine serum albumin

DC:

direct-current

DFM:

dynamic force microscopy

DFS:

dynamic force spectroscopy

DNA:

deoxyribonucleic acid

DTSSP:

3,3′-dithio-bis(sulfosuccinimidylproprionate)

FS:

force spectroscopy

GDP:

guanosine diphosphate

GTP:

guanosine triphosphate

HUVEC:

human umbilical venous endothelial cell

ICAM-1:

intercellular adhesion molecules 1

ICAM-2:

intercellular adhesion molecules 2

IgG:

immunoglobulin G

LFA-1:

leukocyte function-associated antigen-1

MRFM:

magnetic resonance force microscopy

MRFM:

molecular recognition force microscopy

NHS:

N-hydroxysuccinimidyl

NTA:

nitrilotriacetate

OT:

optical tweezers

PDP:

2-pyridyldithiopropionyl

PDP:

pyridyldithiopropionate

PEG:

polyethylene glycol

PSGL-1:

P-selectin glycoprotein ligand-1

RGD:

arginine–glycine–aspartic

SATP:

(S-acetylthio)propionate

SFA:

surface forces apparatus

SFD:

shear flow detachment

TREC:

topography and recognition

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Authors and Affiliations

  1. Institute for Biophysics, University of Linz, Altenbergerstr. 69, 4040, Linz, Austria

    Peter Hinterdorfer & Hermann Gruber

  2. Institute for Biophysics, Altenbergerstr. 69, 4040, Linz, Austria

    Andreas Ebner

  3. Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, 76100, Israel

    Ruti Kapon & Ziv Reich

Authors
  1. Peter Hinterdorfer
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  2. Andreas Ebner
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  3. Hermann Gruber
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  4. Ruti Kapon
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  5. Ziv Reich
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Correspondence to Peter Hinterdorfer .

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  1. Nanoprobe Lab. for Bio- & Nanotechnology, Biomimetics (NLB²), Ohio State University, West 19th Avenue 201, Columbus, 43210-1142, Ohio, USA

    Bharat Bhushan

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Hinterdorfer, P., Ebner, A., Gruber, H., Kapon, R., Reich, Z. (2011). Molecular Recognition Force Microscopy: From Molecular Bonds to Complex Energy Landscapes. In: Bhushan, B. (eds) Nanotribology and Nanomechanics I. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-15283-2_8

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  • DOI: https://doi.org/10.1007/978-3-642-15283-2_8

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