Peptide-Induced Amyloid-Like Conformational Transitions in Proteins

Author:

Egorov Vladimir12ORCID,Grudinina Natalia34,Vasin Andrey15,Lebedev Dmitry2

Affiliation:

1. FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17 Professor Popova Street, Saint-Petersburg 197376, Russia

2. FSBI Petersburg Nuclear Physics Institute, NRC Kurchatov Institute, Orlova Roscha, Gatchina 188300, Russia

3. FSBSI Institute of Experimental Medicine, 12 Akademika Pavlova, Saint-Petersburg 197376, Russia

4. FSBI Federal Almazov Medical Research Centre, 2 Akkuratova Street, St. Saint-Petersburg 197341, Russia

5. Saint-Petersburg State Polytechnical University, 29 Polytechnicheskaya Street, Saint-Petersburg 195251, Russia

Abstract

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.

Funder

Russian Foundation for Basic Research

Publisher

Hindawi Limited

Subject

Biochemistry

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