The influence of protein and interfacial structure on the self-assembly of oriented protein arrays.
These results demonstrate the complexity of factors that impact the self-assembly of protein arrays via the specific binding to receptor-functionalized interfaces. Both the composition and colloidal properties of the protein and target membrane surfaces will affect the protein-surface interactions. However, different structural features control the interactions over different distance regimes and with different consequences. The long-range interactions that control the adsorption kinetics are sensitive not only to the charge on the target surface but also by the topological charge distribution on the protein exterior. Short-range repulsive interactions rooted in both the protein topology and in the membrane structure, by contrast, can significantly alter both the rates and strengths binding. Consequently, the effective design of self-assembling protein arrays must consider not only the recognition interactions that drive such self-organization, but also the details of the micro-environment and their impact on molecular recognition events.
Leckband
D E
DE
Department of Chemical Engineering, University of Illinois at Urbana-Champaign 61801, USA.
D001360:Avidin; D001710:Biotin; D008081:Liposomes / Q000737:chemistry*; D008564:Membrane Potentials; D008961:Models, Structural; D008962:Models, Theoretical; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity; D013499:Surface Properties
D008081:Liposomes; D011506:Proteins; D001360:Avidin; D001710:Biotin