Cooperative adhesion of ligand-receptor bonds

Xiaohui Zhang, Vincent T. Moy

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

Cooperative (simultaneous) breakage of multiple adhesive bonds has been proposed as a mechanism for enhanced binding strength between adhesion molecules on apposing cell surfaces. In this report, we used the atomic force microscopy (AFM) to study how changes in binding affinity and separation rate of force-induced ligand-receptor dissociation affect binding cooperativity. The AFM force measurements were carried out using (strept)avidin-functionalized cantilever tips and biotinylated agarose beads under conditions where multiple (strept)avidin-biotin linkages were formed following surface contact. At slow surface separation of the AFM cantilever from the bead's surface, the (strept)avidin-biotin linkages appeared to rupture sequentially. Increasing the separation rate from 210 to 1950 nm/s led to a linear increase in the average rupture force. Moreover, force histograms revealed a quantized force distribution that shifted toward higher values with increasing separation rate. In measurements of streptavidin-iminobiotin adhesion, the force distribution also shifted toward higher values when the buffer was adjusted to a higher pH to raise the binding affinity. Together, these results demonstrate that the cooperativity of ligand-receptor bonds is significantly enhanced by increases in surface separation rate and/or binding affinity.

Original languageEnglish
Pages (from-to)271-278
Number of pages8
JournalBiophysical Chemistry
Volume104
Issue number1
DOIs
StatePublished - May 1 2003

Fingerprint

Avidin
Atomic Force Microscopy
adhesion
Adhesion
Biotin
Ligands
ligands
Rupture
affinity
force distribution
Atomic force microscopy
biotin
atomic force microscopy
Streptavidin
linkages
beads
Adhesives
Sepharose
Buffers
Force measurement

Keywords

  • Adhesion
  • Atomic force microscopy
  • Bond rupture
  • Ligand-receptor interaction
  • Single molecule interaction

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Biophysics

Cite this

Cooperative adhesion of ligand-receptor bonds. / Zhang, Xiaohui; Moy, Vincent T.

In: Biophysical Chemistry, Vol. 104, No. 1, 01.05.2003, p. 271-278.

Research output: Contribution to journalArticle

Zhang, Xiaohui ; Moy, Vincent T. / Cooperative adhesion of ligand-receptor bonds. In: Biophysical Chemistry. 2003 ; Vol. 104, No. 1. pp. 271-278.
@article{dd544c70118d4bd9affa61e2b41b28c9,
title = "Cooperative adhesion of ligand-receptor bonds",
abstract = "Cooperative (simultaneous) breakage of multiple adhesive bonds has been proposed as a mechanism for enhanced binding strength between adhesion molecules on apposing cell surfaces. In this report, we used the atomic force microscopy (AFM) to study how changes in binding affinity and separation rate of force-induced ligand-receptor dissociation affect binding cooperativity. The AFM force measurements were carried out using (strept)avidin-functionalized cantilever tips and biotinylated agarose beads under conditions where multiple (strept)avidin-biotin linkages were formed following surface contact. At slow surface separation of the AFM cantilever from the bead's surface, the (strept)avidin-biotin linkages appeared to rupture sequentially. Increasing the separation rate from 210 to 1950 nm/s led to a linear increase in the average rupture force. Moreover, force histograms revealed a quantized force distribution that shifted toward higher values with increasing separation rate. In measurements of streptavidin-iminobiotin adhesion, the force distribution also shifted toward higher values when the buffer was adjusted to a higher pH to raise the binding affinity. Together, these results demonstrate that the cooperativity of ligand-receptor bonds is significantly enhanced by increases in surface separation rate and/or binding affinity.",
keywords = "Adhesion, Atomic force microscopy, Bond rupture, Ligand-receptor interaction, Single molecule interaction",
author = "Xiaohui Zhang and Moy, {Vincent T.}",
year = "2003",
month = "5",
day = "1",
doi = "10.1016/S0301-4622(02)00381-2",
language = "English",
volume = "104",
pages = "271--278",
journal = "Biophysical Chemistry",
issn = "0301-4622",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Cooperative adhesion of ligand-receptor bonds

AU - Zhang, Xiaohui

AU - Moy, Vincent T.

PY - 2003/5/1

Y1 - 2003/5/1

N2 - Cooperative (simultaneous) breakage of multiple adhesive bonds has been proposed as a mechanism for enhanced binding strength between adhesion molecules on apposing cell surfaces. In this report, we used the atomic force microscopy (AFM) to study how changes in binding affinity and separation rate of force-induced ligand-receptor dissociation affect binding cooperativity. The AFM force measurements were carried out using (strept)avidin-functionalized cantilever tips and biotinylated agarose beads under conditions where multiple (strept)avidin-biotin linkages were formed following surface contact. At slow surface separation of the AFM cantilever from the bead's surface, the (strept)avidin-biotin linkages appeared to rupture sequentially. Increasing the separation rate from 210 to 1950 nm/s led to a linear increase in the average rupture force. Moreover, force histograms revealed a quantized force distribution that shifted toward higher values with increasing separation rate. In measurements of streptavidin-iminobiotin adhesion, the force distribution also shifted toward higher values when the buffer was adjusted to a higher pH to raise the binding affinity. Together, these results demonstrate that the cooperativity of ligand-receptor bonds is significantly enhanced by increases in surface separation rate and/or binding affinity.

AB - Cooperative (simultaneous) breakage of multiple adhesive bonds has been proposed as a mechanism for enhanced binding strength between adhesion molecules on apposing cell surfaces. In this report, we used the atomic force microscopy (AFM) to study how changes in binding affinity and separation rate of force-induced ligand-receptor dissociation affect binding cooperativity. The AFM force measurements were carried out using (strept)avidin-functionalized cantilever tips and biotinylated agarose beads under conditions where multiple (strept)avidin-biotin linkages were formed following surface contact. At slow surface separation of the AFM cantilever from the bead's surface, the (strept)avidin-biotin linkages appeared to rupture sequentially. Increasing the separation rate from 210 to 1950 nm/s led to a linear increase in the average rupture force. Moreover, force histograms revealed a quantized force distribution that shifted toward higher values with increasing separation rate. In measurements of streptavidin-iminobiotin adhesion, the force distribution also shifted toward higher values when the buffer was adjusted to a higher pH to raise the binding affinity. Together, these results demonstrate that the cooperativity of ligand-receptor bonds is significantly enhanced by increases in surface separation rate and/or binding affinity.

KW - Adhesion

KW - Atomic force microscopy

KW - Bond rupture

KW - Ligand-receptor interaction

KW - Single molecule interaction

UR - http://www.scopus.com/inward/record.url?scp=0038354493&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038354493&partnerID=8YFLogxK

U2 - 10.1016/S0301-4622(02)00381-2

DO - 10.1016/S0301-4622(02)00381-2

M3 - Article

C2 - 12834845

AN - SCOPUS:0038354493

VL - 104

SP - 271

EP - 278

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

IS - 1

ER -