Journal of Physical Chemistry & Biophysics
Open Access

Department of Chemistry, East Carolina University, Greenville, North Carolina, USA

Publications

• Research   
  Distinct Effect of the Pathogenic Mutations on α-Synuclein Aggregation in the Presence of Lipid Vesicles
  Author(s): Anvesh K. R. Dasari, Sungsool Wi, Rakez Kayed and Kwang Hun Lim*
  
  The misfolding and self-assembly of α-synuclein into fibrillar aggregates are closely linked to Parkinson's Disease (PD) and related dementia. Emerging evidence indicates that intermediate states, particularly small oligomers, formed during the misfolding process are the major toxic species. Despite the importance of characterizing these small oligomers to better understand the molecular mechanisms of misfolding, their biophysical study has been hindered by the absence of dependable methods for generating diverse oligomeric forms. In this work, we describe distinct small misfolded oligomers generated from Wild-Type (WT) and pathogenic variants (A53T and G51D ) of α-synuclein, which were produced by using lipid vesicles at pH 7.4. Our findings indicate that single-point mutations affect the aggregation behavior of α-synuclein under .. View More»
  DOI: 10.35841/2161-0398.24.14.410

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