Prion Interaction with Normal Protein in Topological Changing Secondary Structure to Aggregation
Abstract
Prion is a protein smaller than virus and it infects host in the absence of nucleic acid. The secondary structure of protein folds incorrectly from α-helices to β-sheets through breaking and re-formation of hydrogen bond. Structural analogy of α-helix and DNA double helix and comparing differences between α-helix and β-sheet show prion's infectivity and propagation. Aggregates of dimers and polymers generate β-amyloid fibril in Alzheimer's disease.
References
[2] Pravas KB, Jiang Y, Adriano A, et al. Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc). Protein Science 2019; 28(12): 2055-2063.
[3] Banwarth-Kuhn M, Sindi S. How and why to build a mathematical model: A case study using prion aggregation. Journal of Biological Chemistry 2020; 295(15): 5022–5035. doi: 10.1074/jbc.REV119.009851.
[4] Gao Z, Shi J, Cai L, et al. Prion dimer is heterogenous and is modulated by multiple negative and positive motifs. Biochemical & Biophysical Research Communications 2019; 509(2): 570-576. doi: 10.1016/j.bbrc.2018.12.113.
[5] Ma J, Wang F. Prion disease and the 'protein-only hypothesis'. Essays in Biochemistry 2014; 56: 181-191. doi: 10.1042/bse0560181.
Copyright (c) 2020 Yao Yao
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
Authors submitting to USP journals agree to publish their manuscript under the Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0) where authors agree to allow third parties to share their work (copy, distribute, transmit) and to adapt it, under the condition that the authors are given credit, and that in the event of reuse or distribution, the terms of this license are made clear
Authors retain copyright of their work, with first publication rights (online and print) granted to Universe Scientific Publishing or the owner of the journal in question.