Buildup of amyloid fibrils is known to be the cause of certain neurodegenerative disorders. One such disorder is Parkinson’s disease, caused by the misfolding and aggregation of α-synuclein. This protein normally adopts a random coil structure but contains a hydrophobic core that has a propensity to form β-sheets. Prior research has identified five regions that could contain the nucleation side for β-sheet formation. The stretch of peptides 67-71 (GGAVV) is one of these regions, labelled as β-5.<br/>GGA is a naturally disordered tri-peptide found in the β-5 region of α -synuclein. GGA and other tri- and tetra- peptides from this sequence were synthesized using solid-phase peptide synthesis techniques. Using FTIR spectroscopy, interactions between GGA and the other peptides of the 67-71 region were studied. FTIR spectroscopy allows us to differentiate random coil, parallel β-sheet and anti-parallel β-sheet secondary structures by observing the Amide I stretch found in the 1600-1700 cm<sup>-1</sup> range. The frequency of this band is mainly associated with C=O stretching vibrations. As such, it is affected by the amount of H-bonding between the peptide backbone. Combination experiments showed that GGA demonstrated the ability to disrupt β -sheet formation in peptides that naturally take on a β-sheet secondary structure, including AVA and AVV, at equal concentrations.

Preventing aggregation in peptides derived from β-sheet rich sections of α -synuclein

255th National Meeting (2018)

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