Experimental verification of hidden amyloidogenicity of proteins

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K14458
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: Osaka University
• Principal Investigator: Goto Yuji 大阪大学, たんぱく質研究所, 教授 (40153770)
• Co-Investigator(Renkei-kenkyūsha): OGI Hirotsugu 大阪大学, 基礎工学研究科, 准教授 (90252626) ; SAKURAI Kazumasa 近畿大学, 先端技術総合研究所, 准教授 (10403015)
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: 蛋白質 / 脳神経変性疾患 / 生体分子 / 凝集 / 変性 / アミロイド線維 / 溶解度 / 過飽和

Outline of Final Research Achievements

Various proteins form amyloid fibrils and are responsible for amyloidosis. On the other hand, other proteins do not form amyloid fibrils. If we could form amyloid fibrils with those non-amyloid proteins, we can advance our understanding of the mechanism of amyloid formation.
Ovalbumin consisting of 385 amino acid residues is one of the most popular food proteins and does not form amyloid fibrils. We found that a peptide mixture of ovalbumin produced by tryptic digestion contains an amyloidogenic peptide. We purified and determine the amino acid sequence of the amyloidogenic peptide. We also chemically synthesized the peptide and characterized its amyloidogenic properties. The results showed that even ovalbumin contains highly amyloidogenic sequence, although its amyloidogenicity is hidden by the suppressing effects of surrounding sequences.

Free Research Field

蛋白質科学