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Biophysical Journal Volume 105 August 2013 745?Aggregation Modulators Interfere with Membrane Interactions of b2-Microglobulin FibrilsTania Sheynis,? Anat Friediger,6 Wei-Feng Xue,?Andrew L. Hellewell,?Kevin W. Tipping,?Eric W. Hewitt,?Sheena E. Radford,? and Raz JelinekDepartment of Chemistry and Ilse Katz Institute for Nanotechnology, Ben-Gurion University from the Negev, Beer-Sheva, Israel; and �Astbury Centre for Structural Molecular IL-17A Protein Purity & Documentation Biology and School of Molecular and Cellular Biology, University of Leeds, Leeds, United KingdomABSTRACT Amyloid fibril accumulation is a pathological hallmark of a number of devastating disorders, which includes Alzheimer’s illness, prion ailments, sort II diabetes, and others. Even though the molecular factors accountable for amyloid pathologies haven’t been deciphered, interactions of misfolded proteins with cell membranes seem to play vital roles in these problems. Regardless of rising proof for the involvement of membranes in amyloid-mediated cytotoxicity, the pursuit for therapeutic techniques has focused on stopping self-assembly from the proteins comprising the amyloid plaques. Here we present an investigation with the effect of fibrillation modulators upon membrane interactions of b2-microglobulin (b2m) fibrils. The experiments reveal that polyphenols (epigallocatechin gallate, bromophenol blue, and MASP1 Protein Purity & Documentation resveratrol) and glycosaminoglycans (heparin and heparin disaccharide) differentially affect membrane interactions of b2m fibrils measured by dye-release experiments, fluorescence anisotropy of labeled lipid, and confocal and cryo-electron microscopies. Interestingly, whereas epigallocatechin gallate and heparin avert membrane damage as judged by these assays, the other compounds tested had small, or no, effect. The results recommend a new dimension for the biological influence of fibrillation modulators that includes interference with membrane interactions of amyloid species, adding to modern strategies for combating amyloid ailments that concentrate on disruption or remodeling of amyloid aggregates.INTRODUCTION The transformation of soluble proteins into amyloid fibrils deposited in different organs and tissues is usually a hallmark of devastating medical problems, like Alzheimer’.
