Amyloid fibril is the protein structure, which resulted from its improper folding into secondary structure of beta-sheet. There are several diseases in which amyloid fibril formation is the main cause of the disease. The list of these diseases includes Alzheimer's disease, where the main protein responsible for misfolding is the amyloid-� peptide; type II diabetes with the islet amyloid polypeptide, Parkinson's disease with a-synuclein protein, as well as Creutzfeldt-Jakob disease, chronic inflammation amyloidosis and prion disease. We study aggregation of short peptide fragment NFGAILSS which was determined in previous works as one of the units causing the aggregation in Amylin or Islet Amyloid Peptide (IAPP). The purpose of the experiment is to determine the affect of different conditions such as salt NaCl concentrations, various pH and viscosity on the NFGAILSS. Aggregation rates were determined by using UV turbidity measurements at 405nm. The results of the experiment showed that the different environments influence aggregation of the peptide. The determination of the inhibitor of the aggregation will give the insight into the design of the drug for the type II diabetes.

Peptide aggregation using UV-spectroscopy

248th National Meeting (2014)

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