Adhesion forces between individual ligand-receptor pairs - PubMed (original) (raw)
. 1994 Apr 15;264(5157):415-7.
doi: 10.1126/science.8153628.
Affiliations
- PMID: 8153628
- DOI: 10.1126/science.8153628
Adhesion forces between individual ligand-receptor pairs
E L Florin et al. Science. 1994.
Abstract
The adhesion force between the tip of an atomic force microscope cantilever derivatized with avidin and agarose beads functionalized with biotin, desthiobiotin, or iminobiotin was measured. Under conditions that allowed only a limited number of molecular pairs to interact, the force required to separate tip and bead was found to be quantized in integer multiples of 160 +/- 20 piconewtons for biotin and 85 +/- 15 piconewtons for iminobiotin. The measured force quanta are interpreted as the unbinding forces of individual molecular pairs.
Similar articles
- Cooperative adhesion of ligand-receptor bonds.
Zhang X, Moy VT. Zhang X, et al. Biophys Chem. 2003 May 1;104(1):271-8. doi: 10.1016/s0301-4622(02)00381-2. Biophys Chem. 2003. PMID: 12834845 - Adhesion energy of receptor-mediated interaction measured by elastic deformation.
Moy VT, Jiao Y, Hillmann T, Lehmann H, Sano T. Moy VT, et al. Biophys J. 1999 Mar;76(3):1632-8. doi: 10.1016/S0006-3495(99)77322-4. Biophys J. 1999. PMID: 10049343 Free PMC article. - Unbinding molecular recognition force maps of localized single receptor molecules by atomic force microscopy.
Sotres J, Lostao A, Wildling L, Ebner A, Gómez-Moreno C, Gruber HJ, Hinterdorfer P, Baró AM. Sotres J, et al. Chemphyschem. 2008 Mar 14;9(4):590-9. doi: 10.1002/cphc.200700597. Chemphyschem. 2008. PMID: 18297676 - Molecular dynamics study of unbinding of the avidin-biotin complex.
Izrailev S, Stepaniants S, Balsera M, Oono Y, Schulten K. Izrailev S, et al. Biophys J. 1997 Apr;72(4):1568-81. doi: 10.1016/S0006-3495(97)78804-0. Biophys J. 1997. PMID: 9083662 Free PMC article. - Force: a new structural control parameter?
Bensimon D. Bensimon D. Structure. 1996 Aug 15;4(8):885-9. doi: 10.1016/s0969-2126(96)00095-0. Structure. 1996. PMID: 8805575 Review.
Cited by
- Nanomechanical thermometry for probing sub-nW thermal transport.
Oh S, Shekhawat NS, Jameel O, Lal A, Lee CH. Oh S, et al. Microsyst Nanoeng. 2024 Oct 18;10(1):148. doi: 10.1038/s41378-024-00770-w. Microsyst Nanoeng. 2024. PMID: 39420179 Free PMC article. - Applying the Atomic Force Microscopy Technique in Medical Sciences-A Narrative Review.
Krawczyk-Wołoszyn K, Roczkowski D, Reich A, Żychowska M. Krawczyk-Wołoszyn K, et al. Biomedicines. 2024 Sep 3;12(9):2012. doi: 10.3390/biomedicines12092012. Biomedicines. 2024. PMID: 39335524 Free PMC article. Review. - Nanocellulose-Bovine Serum Albumin Interactions in an Aqueous Medium: Investigations Using In Situ Nanocolloidal Probe Microscopy and Reactive Molecular Dynamics Simulations.
Khalili H, Monti S, Pesquet E, Jaworski A, Lombardo S, Mathew AP. Khalili H, et al. Biomacromolecules. 2024 Jun 10;25(6):3703-3714. doi: 10.1021/acs.biomac.4c00264. Epub 2024 May 28. Biomacromolecules. 2024. PMID: 38806282 Free PMC article. - Understanding Emergent Complexity from a Single-Molecule Perspective.
Guo Y, Li M, Zhao C, Zhang Y, Jia C, Guo X. Guo Y, et al. JACS Au. 2024 Mar 20;4(4):1278-1294. doi: 10.1021/jacsau.3c00845. eCollection 2024 Apr 22. JACS Au. 2024. PMID: 38665639 Free PMC article. Review. - Determination of single-molecule loading rate during mechanotransduction in cell adhesion.
Jo MH, Meneses P, Yang O, Carcamo CC, Pangeni S, Ha T. Jo MH, et al. Science. 2024 Mar 22;383(6689):1374-1379. doi: 10.1126/science.adk6921. Epub 2024 Mar 21. Science. 2024. PMID: 38513010 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources