title: Disulfide bonds in amyloidogenesis diseases related proteins.
abstract: More than 20 human diseases, including Alzheimer's disease, Parkinson's disease, and prion disease, originate from the deposition of misfolded proteins. These proteins, referred as amyloidogenic proteins, adopt a β-sheet-rich structure when transformed from soluble state into insoluble amyloid fibrils. Amyloid formation is influenced by a number of factors that affect the intermolecular interaction, including pH, temperature, ion strength, and chemical bonds. In this review, we focus on the role of disulfide on the stability, structure, oligomerization, and amyloidogenecity of native folded or unfolded amyloidogenic proteins. The effects of introduced disulfide bonds on the amyloidogenicity of proteins lacking native disulfide are also reviewed.
authors.affiliation: Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, People's Republic of China, 430030.
authors.forename: Yang
authors.initials: Y
authors.lastname: Li
authors.forename: Juan
authors.initials: J
authors.lastname: Yan
authors.forename: Xin
authors.initials: X
authors.lastname: Zhang
authors.forename: Kun
authors.initials: K
authors.lastname: Huang
mesh_terms: D000682:Amyloid / Q000737:chemistry; D058227:Amyloidogenic Proteins / Q000737:chemistry*; D000818:Animals; D004220:Disulfides / Q000737:chemistry*; D006801:Humans; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D058227:Amyloidogenic Proteins; D004220:Disulfides
keywords: amyloid fibrils; disulfide; oligomers; stability; structure