Table of Contents
International Journal of Peptides
Volume 2015, Article ID 723186, 5 pages
Review Article

Peptide-Induced Amyloid-Like Conformational Transitions in Proteins

1FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17 Professor Popova Street, Saint-Petersburg 197376, Russia
2FSBI Petersburg Nuclear Physics Institute, NRC Kurchatov Institute, Orlova Roscha, Gatchina 188300, Russia
3FSBSI Institute of Experimental Medicine, 12 Akademika Pavlova, Saint-Petersburg 197376, Russia
4FSBI Federal Almazov Medical Research Centre, 2 Akkuratova Street, St. Saint-Petersburg 197341, Russia
5Saint-Petersburg State Polytechnical University, 29 Polytechnicheskaya Street, Saint-Petersburg 195251, Russia

Received 17 May 2015; Revised 3 August 2015; Accepted 4 August 2015

Academic Editor: Hubert Vaudry

Copyright © 2015 Vladimir Egorov et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function.