Effect of Urea, Arginine, and Ethanol Concentration on Aggregation of ₁₇₉CVNITV₁₈₄ Fragment of Sheep Prion Protein.

ABSTRACT: Understanding protein aggregation is of utmost importance as it is responsible for causing several neurodegenerative diseases and one of the serious impediments in large-scale biopharmaceutical production. The prion protein is responsible for pathological states in fatal transmissible spongiform conditions, such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. The peptide fragment 178-191 of Syrian hamster prion protein is known to be amyloidogenic. Here, we identified the fragment ₁₇₉CVNITV₁₈₄ as an aggregation-prone fragment in sheep prion protein. This fragment is conserved sequence among sheep and Syrian hamster prion protein and also falls in the previously identified amyloidogenic sequence. The mechanistic details of the aggregation behavior ar

SUBMITTER: Jahan I 

PROVIDER: S-EPMC6173503 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature