A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV-1 V3 loop

FEBS Letters
Chrysoula KokotidouAnna Mitraki

Abstract

The GAIIG sequence, common to the amyloid beta peptide (residues 29-33) and to the HIV-1 gp120 (residues 24-28 in a typical V3 loop), self-assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self-assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid-based materials. Moreover, we report the single crystal X-ray structure of the beta-breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure-based design of potential inhibitors of amyloid formation.

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Citations

Dec 22, 2019·Biomolecules·Chrysoula KokotidouAnd Anna Mitraki
Sep 13, 2018·International Journal of Molecular Sciences·Sofia GiorgettiFrancesco Antonio Aprile
Nov 28, 2020·Cellular and Molecular Life Sciences : CMLS·Emiel MichielsJoost Schymkowitz
Nov 6, 2018·International Journal of Biological Macromolecules·Suparna KhatunAmar Nath Gupta
Dec 29, 2019·The Journal of Physical Chemistry. B·Sai Vamshi R JonnalagaddaManos Gkikas
Dec 7, 2019·Journal of Chemical Information and Modeling·Joseph M JakubowskiPhanourios Tamamis
Jul 23, 2020·The Journal of Physical Chemistry. B·Anastassia N RissanouAnna Mitraki
Jul 6, 2018·The Journal of Physical Chemistry. B·Sai Vamshi R JonnalagaddaPhanourios Tamamis

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