Tuning the conformational properties of the prion peptide

Proteins
Chai-Chi HoRita P-Y Chen

Abstract

Previously, we disclosed that O-linked glycosylation of Ser-132 or Ser-135 could dramatically change the amyloidogenic property of the hamster prion peptide (sequence 108-144). This peptide, which corresponds to the flexible loop and the first beta-strand in the structure of the prion protein, is a random coil when it is initially dissolved in buffer, but amyloid fibrils are formed with time. Thus, it offers a convenient model system to observe and compare how different chemical modifications and sequence mutations alter the amyloidogenic property of the peptide within a reasonable experimental time frame. In our earlier study, aside from uncovering a site-specificity of the glycosylation on the fibrillogenesis, different effects of alpha-GalNAc and beta-GlcNAc were observed. In this work, we explore further how different sugar configurations affect the conformational property of the polypeptide chain. We compare the effects of O-linked glycosylation by the common sugars alpha-GalNAc, beta-GlcNAc with their non-native analogs beta-GalNAc, alpha-GlcNAc in an effort to uncover the origin of the sugar-specificity on the fibril formation. We find that the anomeric configuration of the sugar is the most important factor affecting th...Continue Reading

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Citations

Feb 19, 2016·Chemistry : a European Journal·Moran Frenkel-PinterDaniel Segal
Apr 25, 2014·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Xiaoyan LiuLianwen Zhang
Nov 1, 2020·International Journal of Biological Macromolecules·Yoshito AbeTadashi Ueda
Feb 27, 2020·Chemical Reviews·Moran Frenkel-PinterLuke J Leman

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