Amyloidogenic peptide homologous to fragment 129–148 of human myocilin

Vladimir V. Egorov Research Institute of Influenza; Ministry of Healthcare of the Russian Federation; St. Petersburg, Russia; Kurchatov Institute; Petersburg Nuclear Physics Institute; Gatchina, RussiaCorrespondence[email protected]

Natalia A. Grudinina Institute of Experimental Medicine RAMS; St. Petersburg, Russia

Dmitry V. Lebedev Kurchatov Institute; Petersburg Nuclear Physics Institute; Gatchina, Russia

Aram A. Shaldzhyan Research Institute of Influenza; Ministry of Healthcare of the Russian Federation; St. Petersburg, Russia

Alexander V. Slita Research Institute of Influenza; Ministry of Healthcare of the Russian Federation; St. Petersburg, Russia

Alexey K. Sirotkin Research Institute of Influenza; Ministry of Healthcare of the Russian Federation; St. Petersburg, Russia

Andrey V. Vasin Research Institute of Influenza; Ministry of Healthcare of the Russian Federation; St. Petersburg, Russia

Michael M. Shavlovsky Institute of Experimental Medicine RAMS; St. Petersburg, Russia

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Abstract

Myocilin is a protein with a molecular weight near 50 kDa. It is expressed in almost all organs and tissues.Citation¹ We showed that the peptide DQL ETQ TRE LET AYS NLL RD corresponding to N-terminal Leucine zipper motif (LZM) of the protein is able to form amyloid-like fibrils. The possible role of this motif in myocilin aggregation is discussed.

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Disclosure of Potential Conflicts of Interest

No potential conflicts of interest were disclosed.

Acknowledgments

This study is supported by RFBR grants Nº09-04-00788-a, 07-04-01454-a, 07-04-00476-a.

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Amyloidogenic peptide homologous to fragment 129–148 of human myocilin

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Amyloidogenic peptide homologous to fragment 129–148 of human myocilin

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Disclosure of Potential Conflicts of Interest

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