Tunable aggregation by competing biomolecular interactions
Measurements and models are reported for Concanavalin A (ConA) mediated aggregation of dextran coated colloids that is tunable via a competing ConA-glucose interaction. Video and confocal scanning laser microscopy were used to characterize ConA adsorption to dextran colloids and quasi-2D dextran coa...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 30(2014), 50 vom: 23. Dez., Seite 15253-60 |
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Format: | Online-Aufsatz |
Sprache: | English |
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2014
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. Dextrans Concanavalin A 11028-71-0 Glucose IY9XDZ35W2 |
Zusammenfassung: | Measurements and models are reported for Concanavalin A (ConA) mediated aggregation of dextran coated colloids that is tunable via a competing ConA-glucose interaction. Video and confocal scanning laser microscopy were used to characterize ConA adsorption to dextran colloids and quasi-2D dextran coated colloid aggregation kinetics vs [ConA] and [glucose]. ConA adsorption to, and aggregation rates of, dextran coated colloids increased from negligible values to high coverage and rapid rates for increasing [ConA] in the range 0.1-10 mM and decreasing [glucose] in the range 1-100 mM, consistent with dissociation constant estimates. Analysis of colloidal aggregation kinetics indicates ConA bridge formation is the rate-limiting step controlling the transition from slow to rapid aggregation. Our findings reveal a mechanism for tuning colloidal interactions and aggregation kinetics through specific, competitive biomolecular interactions, which lends insights into aggregation phenomena in mixed synthetic-biomaterial and biological systems |
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Beschreibung: | Date Completed 13.08.2015 Date Revised 25.11.2016 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/la503772g |