A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis

Vladimir V Egorov; Dmitry V Lebedev; Aram A Shaldzhyan; Alexey K Sirotkin; Andrey N Gorshkov; Olga A Mirgorodskaya; Natalia A Grudinina; Andrey V Vasin; Michael M Shavlovsky

doi:10.4161/19336896.2014.983745

A conservative mutant of a proteolytic fragment produced during fibril formation enhances fibrillogenesis

Prion. 2014;8(5):369-73. doi: 10.4161/19336896.2014.983745.

Authors

Vladimir V Egorov¹, Dmitry V Lebedev, Aram A Shaldzhyan, Alexey K Sirotkin, Andrey N Gorshkov, Olga A Mirgorodskaya, Natalia A Grudinina, Andrey V Vasin, Michael M Shavlovsky

Affiliation

¹ a FSBI Research Institute of Influenza; Ministry of Healthcare of the Russian Federation ; St. Petersburg , Russia.

Abstract

The fibrillogenesis of a peptide corresponding to residues 35-51 of human α-lactalbumin (¹GYDTQAIVENNESTEYG¹⁷) can be dramatically enhanced by the addition of a tetrapeptide TDYG homologous to its C-terminus (TEYG). Generation of spontaneous hydrolytic products similar to this peptide was demonstrated by mass-spectrometry analysis of GYDTQAIVENNESTEYG peptide solution components during fibrillogenesis. Possible mechanisms and roles of short peptides in protein metabolism are discussed.

Keywords: Fibrillogenesis; GYDTQAIVENNESTEYG; conformation transmission; lactalbumin; short peptides; spontaneous hydrolysis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amyloid / chemistry
Amyloid / genetics*
Amyloid / ultrastructure
Humans
Microscopy, Electron, Transmission
Molecular Sequence Data
Mutation*
Proteolysis

Substances

Amyloid