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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Celik, Emrah Moy, Vincent T. |
| Description | Country affiliation: United States Author Affiliation: Celik E ( Department of Physiology and Biophysics, University of Miami School of Medicine, Miami, FL 33136, USA. ecelik@med.miami.edu) |
| Abstract | Sample-probe contact duration (dwell time) and loading force are two important parameters for the atomic force microscopy (AFM) force spectroscopy measurements of ligand-receptor interaction. A prolonged contact time may be required to initiate ligand-receptor binding as a result of slow on-rate kinetics or low reactant density. In general, increasing contact duration promotes nonspecific interactions between the substrate and the functionalized cantilever and, thus, masking the detection of the specific interactions. To reduce the nonspecific interactions in AFM force measurements requiring extended substrate-probe contact, we investigated the interaction of bovine serum albumin (BSA)-functionalized cantilever with BSA-coated glass, polyethylene glycol (PEG)-functionalized glass, Pluronic-treated Petri dishes and agarose beads. The frequency of nonspecific interaction between the BSA-functionalized cantilever and the different samples increased with loading force and dwell time. This increase in nonspecific adhesion can be attributed to the interaction mediated by forced unfolding of BSA. By reducing the loading force, the contact duration of the AFM probe with an agarose bead can be extended to a few minutes without nonspecific adhesion. |
| File Format | HTM / HTML |
| ISSN | 09523499 |
| Issue Number | 1 |
| Volume Number | 25 |
| e-ISSN | 10991352 |
| Journal | Journal of Molecular Recognition |
| Language | English |
| Publisher | Wiley |
| Publisher Date | 2012-01-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Molecular Biology Microscopy, Atomic Force Methods Polyethylene Glycols Chemistry Proteins Sepharose Serum Albumin, Bovine Adsorption Glass Microspheres Surface Properties Journal Article Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology |
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