The time dependence of the adsorption of myelin basic protein onto dipalmitoyl phosphatidyl glycerol multilayers has been followed directly, using a novel application of a microgravimetric gauge. Our results, supplemented by other data obtained by FTIR, show the ease and versatility of the quartz microbalance for investigating the interaction processes between proteins and phospholipid layers and show that the protein adsorption is accompanied by structural changes in the proteolipid ensemble and adsorbed liquid water; it is furthermore dependent on the mesoscopic defect morphology of the ensemble.
Kinetics of the interaction of myelin basic protein with phospholipid layers
Facci P;
1999
Abstract
The time dependence of the adsorption of myelin basic protein onto dipalmitoyl phosphatidyl glycerol multilayers has been followed directly, using a novel application of a microgravimetric gauge. Our results, supplemented by other data obtained by FTIR, show the ease and versatility of the quartz microbalance for investigating the interaction processes between proteins and phospholipid layers and show that the protein adsorption is accompanied by structural changes in the proteolipid ensemble and adsorbed liquid water; it is furthermore dependent on the mesoscopic defect morphology of the ensemble.File in questo prodotto:
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