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

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:

• conformation transmission
• Fibrillogenesis
• GYDTQAIVENNESTEYG
• lactalbumin
• short peptides
• spontaneous hydrolysis

Disclosure of Potential Conflicts of Interest

No potential conflicts of interest were disclosed.

Acknowledgments

The authors wish to thank Brian Hoettels for his help in the manuscript preparation.

Funding

This work was supported by the federal target program “Scientific and Scientific-Pedagogical Personnel of Innovative Russia” for 2009–2013 (activity 1.5, agreement 8482) and partially supported by RFBR, research project No.14-24-01103.