Journal article

Dimeric structures of alpha-synuclein bind preferentially to lipid membranes

Eleni Giannakis, Jessica Pacifico, David P Smith, Lin Wai Hung, Colin L Masters, Roberto Cappai, John D Wade, Kevin J Barnhain

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | ELSEVIER | Published : 2008

Abstract

There is substantial evidence which implicates alpha-synuclein and its ability to aggregate and bind vesicle membranes as critical factors in the development of Parkinson's disease. In order to investigate the interaction between alpha-synuclein wild type (Wt) and its familial mutants, A53T and A30P with lipid membranes, we developed a novel lipid binding assay using surface enhanced laser desorption/ionisation-time of flight-mass spectrometry (SELDI-TOF MS). Wt and A53T exhibited similar lipid binding profiles; monomeric species and dimers bound with high relative affinity to the lipid surface, the latter of which exhibited preferential binding. Wt and A53T trimers and tetramers were also d..

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