Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy

C. Yuan, A. Chen, P. Kolb, Vincent T. Moy

Research output: Contribution to journalArticle

225 Citations (Scopus)

Abstract

The dissociation of ligand and receptor involves multiple transitions between intermediate states formed during the unbinding process. In this paper, we explored the energy landscape of the streptavidin-biotin interaction by using the atomic force microscope (AFM) to measure the unbinding dynamics of individual ligand-receptor complexes. The rupture force of the streptavidin-biotin bond increased more than 2-fold over a range of loading rates between 100 and 5000 pN/s. Moreover, the force measurements showed two regimes of loading in the streptavidin-biotin force spectrum, revealing the presence of two activation barriers in the unbinding process. Parallel experiments carried out with a streptavidin mutant (W120F) were used to investigate the molecular determinants of the activation barriers. From these experiments, we attributed the outer activation barrier in the energy landscape to the molecular interaction of the '3-4' loop of streptavidin that closes behind biotin.

Original languageEnglish
Pages (from-to)10219-10223
Number of pages5
JournalBiochemistry
Volume39
Issue number33
DOIs
StatePublished - Aug 22 2000

Fingerprint

Streptavidin
Atomic Force Microscopy
Atomic force microscopy
Biotin
Chemical activation
Ligands
Molecular interactions
Force measurement
Rupture
Microscopes
Experiments
biotin-streptavidin complex

ASJC Scopus subject areas

  • Biochemistry

Cite this

Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. / Yuan, C.; Chen, A.; Kolb, P.; Moy, Vincent T.

In: Biochemistry, Vol. 39, No. 33, 22.08.2000, p. 10219-10223.

Research output: Contribution to journalArticle

Yuan, C. ; Chen, A. ; Kolb, P. ; Moy, Vincent T. / Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. In: Biochemistry. 2000 ; Vol. 39, No. 33. pp. 10219-10223.
@article{715509b8ff51416397c6f4414a9ef351,
title = "Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy",
abstract = "The dissociation of ligand and receptor involves multiple transitions between intermediate states formed during the unbinding process. In this paper, we explored the energy landscape of the streptavidin-biotin interaction by using the atomic force microscope (AFM) to measure the unbinding dynamics of individual ligand-receptor complexes. The rupture force of the streptavidin-biotin bond increased more than 2-fold over a range of loading rates between 100 and 5000 pN/s. Moreover, the force measurements showed two regimes of loading in the streptavidin-biotin force spectrum, revealing the presence of two activation barriers in the unbinding process. Parallel experiments carried out with a streptavidin mutant (W120F) were used to investigate the molecular determinants of the activation barriers. From these experiments, we attributed the outer activation barrier in the energy landscape to the molecular interaction of the '3-4' loop of streptavidin that closes behind biotin.",
author = "C. Yuan and A. Chen and P. Kolb and Moy, {Vincent T.}",
year = "2000",
month = "8",
day = "22",
doi = "10.1021/bi992715o",
language = "English",
volume = "39",
pages = "10219--10223",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "33",

}

TY - JOUR

T1 - Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy

AU - Yuan, C.

AU - Chen, A.

AU - Kolb, P.

AU - Moy, Vincent T.

PY - 2000/8/22

Y1 - 2000/8/22

N2 - The dissociation of ligand and receptor involves multiple transitions between intermediate states formed during the unbinding process. In this paper, we explored the energy landscape of the streptavidin-biotin interaction by using the atomic force microscope (AFM) to measure the unbinding dynamics of individual ligand-receptor complexes. The rupture force of the streptavidin-biotin bond increased more than 2-fold over a range of loading rates between 100 and 5000 pN/s. Moreover, the force measurements showed two regimes of loading in the streptavidin-biotin force spectrum, revealing the presence of two activation barriers in the unbinding process. Parallel experiments carried out with a streptavidin mutant (W120F) were used to investigate the molecular determinants of the activation barriers. From these experiments, we attributed the outer activation barrier in the energy landscape to the molecular interaction of the '3-4' loop of streptavidin that closes behind biotin.

AB - The dissociation of ligand and receptor involves multiple transitions between intermediate states formed during the unbinding process. In this paper, we explored the energy landscape of the streptavidin-biotin interaction by using the atomic force microscope (AFM) to measure the unbinding dynamics of individual ligand-receptor complexes. The rupture force of the streptavidin-biotin bond increased more than 2-fold over a range of loading rates between 100 and 5000 pN/s. Moreover, the force measurements showed two regimes of loading in the streptavidin-biotin force spectrum, revealing the presence of two activation barriers in the unbinding process. Parallel experiments carried out with a streptavidin mutant (W120F) were used to investigate the molecular determinants of the activation barriers. From these experiments, we attributed the outer activation barrier in the energy landscape to the molecular interaction of the '3-4' loop of streptavidin that closes behind biotin.

UR - http://www.scopus.com/inward/record.url?scp=0034702770&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034702770&partnerID=8YFLogxK

U2 - 10.1021/bi992715o

DO - 10.1021/bi992715o

M3 - Article

C2 - 10956011

AN - SCOPUS:0034702770

VL - 39

SP - 10219

EP - 10223

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 33

ER -