Diffusing colloidal probes of protein-carbohydrate interactions

We present diffusing colloidal probe measurements of weak, multivalent, specific protein-polysaccharide interactions mediated by a competing monosaccharide. Specifically, we used integrated evanescent wave and video microscopy methods to monitor the three-dimensional Brownian excursions of conconavi...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 29(2013), 7 vom: 19. Feb., Seite 2299-310
1. Verfasser: Eichmann, Shannon L (VerfasserIn)
Weitere Verfasser: Meric, Gulsum, Swavola, Julia C, Bevan, Michael A
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Carbohydrates Colloids Dextrans Proteins Serum Albumin, Bovine 27432CM55Q
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520 |a We present diffusing colloidal probe measurements of weak, multivalent, specific protein-polysaccharide interactions mediated by a competing monosaccharide. Specifically, we used integrated evanescent wave and video microscopy methods to monitor the three-dimensional Brownian excursions of conconavilin A (ConA) decorated colloids interacting with dextran-functionalized surfaces in the presence of glucose. Particle trajectories were interpreted as binding lifetime histograms, binding isotherms, and potentials of mean force. Binding lifetimes and isotherms showed clear trends of decreasing ConA-dextran-specific binding with increasing glucose concentration, consistent with expectations. Net potentials were accurately captured by superposition of a short-range, glucose-independent ConA-dextran repulsion and a longer-range, glucose-dependent dextran bridging attraction modeled as a harmonic potential. For glucose concentrations greater than 100 mM, the net ConA-dextran potential was found to have only a nonspecific repulsion, similar to that of bovine serum albumin (BSA) decorated colloids over dextran determined in control experiments. Our results demonstrate the first use of optical microscopy methods to quantify the connections between potentials of mean force and the binding behavior of ConA-decorated colloids on dextran-functionalized surfaces 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 7 |a Carbohydrates  |2 NLM 
650 7 |a Colloids  |2 NLM 
650 7 |a Dextrans  |2 NLM 
650 7 |a Proteins  |2 NLM 
650 7 |a Serum Albumin, Bovine  |2 NLM 
650 7 |a 27432CM55Q  |2 NLM 
700 1 |a Meric, Gulsum  |e verfasserin  |4 aut 
700 1 |a Swavola, Julia C  |e verfasserin  |4 aut 
700 1 |a Bevan, Michael A  |e verfasserin  |4 aut 
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