SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly

• DOI: 10.1016/j.celrep.2012.06.012
• Publication Date: 2012-07-26T15:22:18Z
• Authors: S. Fabio Falsone; N. Helge Meyer; Evelyne Schrank; Gerd Leitinger; Chi L.L. Pham; Michelle T. Foder...; Mats Holmberg; Martin Dulle; Benjamin Scicluna; Bernd Gesslbauer; Hanna-Marie Rückert; Gabriel E. Wagner; David A. Merle; Ellen A. Nollen; Andreas J. Kungl; Andrew F. Hill; Roberto Cappai; Klaus Zangger
• Keywords: Amyloid (mycology); P3 peptide

The inherent cytotoxicity of aberrantly folded protein aggregates contributes substantially to the pathogenesis amyloid diseases.It was recently shown that a class evolutionary conserved proteins, called MOAG-4/SERF, profoundly alter toxicity via an autonomous but yet unexplained mode.We show biological function human SERF1a originates from its atypical ability specifically distinguish between and nonamyloid aggregation.This inherently unstructured directly affected aggregation kinetics broad range amyloidogenic proteins in vitro, while being inactive against aggregation.A representative biophysical analysis SERF1a:a-synuclein (aSyn) complex revealed amyloid-promoting activity resulted early transient interaction, which sufficient provoke massive increase soluble aSyn nucleation templates.Therefore, amyloid-modifying observed living organisms relies on direct dedicated manipulation stages pathway.