|Title:||Kinetics and enthalpy measurements of interaction between £]-amyloid and liposomes by surface plasmon resonance and isothermal titration microcalorimetry||Authors:||Lin M.-S.
|Keywords:||£]-Amyloid (A£]);Enthalpy;Isothermal titration calorimetry;Lipsome;Surface plasmon resonance||Issue Date:||2007||Journal Volume:||58||Journal Issue:||2||Start page/Pages:||231-236||Source:||Colloids and Surfaces B: Biointerfaces||Abstract:||
The objective of this research is to understand the interaction mechanism of £]-amyloid (A£]) with cell and were basically divided into two parts. The first part focused on the time-dependent structural changes of A£] (1-40) by circular dichroism (CD) spectroscopy, thioflavin T (ThT) fluorescence assay, and atomic force microscopy (AFM). The second part emphasized the kinetics and enthalpy of interaction between A£] (1-40) and liposome by surface plasmon resonance (SPR) and isothermal titration microcalorimetry (ITC). Results obtained from CD, ThT and AFM confirmed the formation of 1 £gm fibril after single day incubation. The driving force of kinetic interaction between A£] and liposomes was revealed by SPR to be electrostatics. Further studies indicated that fresh A£] has high GM1 affinity. Besides, addition of cholesterol to the liposome could alter membrane fluidity and affect the interactions of fresh A£] with liposomes especially in the amount of A£] absorbed and preserving the structure of liposome after adsorbing. Hydrophobicity was found to be the driving force leading to the interaction between A£] fibrils and liposomes. These reactions are endothermic as supported by ITC measurements. When the composition of liposomes is zwitterionic lipids, the interaction of A£] with liposomes is predominantly hydrophobic force. In contrast, the driving force of interaction of charged lipids with A£] is electrostatic. ? 2007 Elsevier B.V. All rights reserved.
|Appears in Collections:||化學工程學系|
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