This research aims to better understand interactions specific to polyglutamine peptide aggregation. There are a number of human, neuromuscular diseases in which it is thought the pathology results from the aggregates. One of these diseases is Huntington’s Disease, a polyQ disease. We employed solid phase peptide synthesis (SPPS) to have synthetic control over the polypeptides studied. Polypeptides synthesized intracellularly use exclusively the L-amino acids, therefore polyglutamine peptides involved in polyQ disease contain only the L-amino acid. To investigate the effect of the enantiomeric alpha-carbon configuration on aggregation, the synthesis of polyglutamine peptides was performed and D-Glutamine (D-Gln) was used as a replacement for some of the L-Glutamine (L-Gln) residues. First, chains of six L-Gln amino acids were produced with a 0.9% and 31% crude yield, respectively. Next, a six amino acid length chain was synthesize with alternating D- and L-Gln residues, resulting in a 5% crude yield. Ultra performance liquid chromatography-mass spectroscopy (UPLC-MS) was used to purify and confirm chain length.

L- and D- glutamine peptide synthesis: Microscale

255th National Meeting (2018)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.