Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 141, Issue 6, Pages 2577-2588Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b12553
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Funding
- Marie Curie Career Integration Grant CELLMULTIVINT [PCIG09-GA-2011-293803]
- European Research Council Starting Grant JELLY [306435]
- CAS PIFI Fellowship
- Natural Science Foundation of China (NSFC) [1181101172]
- Slovenian Research Agency (ARRS) [Z1-9170]
- European Union's Horizon 2020 programme under ETN [674979-NANOTRANS]
- EPSRC
- European Research Council (ERC) [306435] Funding Source: European Research Council (ERC)
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The interaction between a biological membrane and its environment is a complex process, as it involves multivalent binding between ligand/receptor pairs, which can self-organize in patches. Any description of the specific binding of biomolecules to membranes must account for the key characteristics of multivalent binding, namely, its unique ability to discriminate sharply between high and low receptor densities (superselectivity), but also for the effect of the lateral mobility of membrane-bound receptors to cluster upon binding. Here we present an experimental model system that allows us to compare systematically the effects of multivalent interactions on fluid and immobile surfaces. A crucial feature of our model system is that it allows us to control the membrane surface chemistry, the properties of the multivalent binder, and the binding affinity. We find that multivalent probes retain their superselective binding behavior at fluid interfaces. Supported by numerical simulations, we demonstrate that, as a consequence of receptor clustering, superselective binding is enhanced and shifted to lower receptor densities at fluid interfaces. To translate our findings into a simple, predictive tool, we propose an analytical model that enables rapid predictions of how the superselective binding behavior is affected by the lateral receptor mobility as a function of the physicochemical characteristics of the multivalent probe. We believe that our model, which captures the key physical mechanisms underpinning multivalent binding to biological membranes, will greatly facilitate the rational design of nanoprobes for the superselective targeting of cells.
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