Abstract
Alpha-synuclein is intrinsically disordered in solution but adopts a partially alpha-helical structure when membrane bound; we are currently investigating this structure using a cyanylated cysteine vibrational probe at various sites on the αS membrane binding domain. In order to quantitatively understand the depth dependence of the SCN probe in a lipid bilayer, four variants of a poly-L transmembrane helical peptide were designed and synthesized with cysteine residues at different depths in a membrane bilayer. A nonaqueous cyanylation and purification protocol was developed to introduce the probe group on these very hydrophobic model peptides. Vibrational spectroscopy was carried out on the four variants in a model lipid system using both solution/vesicle and oriented, immobilized samples. These data will help to elucidate the membrane interactions of both αS and other membrane-bound proteins.
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