Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology

Magdalena I Ivanova; Yuxi Lin; Young-Ho Lee; Jie Zheng; Ayyalusamy Ramamoorthy

doi:10.1016/j.bpc.2020.106507

Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology

Biophys Chem. 2021 Feb:269:106507. doi: 10.1016/j.bpc.2020.106507. Epub 2020 Nov 19.

Authors

Magdalena I Ivanova¹, Yuxi Lin², Young-Ho Lee³, Jie Zheng⁴, Ayyalusamy Ramamoorthy⁵

Affiliations

¹ Neurology, University of Michigan, Ann Arbor, MI 48109, USA; Biophysics, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: mivanova@umich.edu.
² Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Chungbuk 28119, South Korea.
³ Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Chungbuk 28119, South Korea; Bio-Analytical Science, University of Science and Technology, Daejeon 34113, South Korea; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, South Korea; Research headquarters, Korea Brain Research Institute, Daegu 41068, South Korea.
⁴ Department of Chemical and Biomolecular Engineering, The University of Akron, Ohio, USA.
⁵ Biophysics, University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Macromolecular Science and Engineering, University of Michigan, Ann Arbor, MI 48109, USA; Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: ramamoor@umich.edu.

Abstract

Abnormal aggregation of proteins into filamentous aggregates commonly associates with many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes. These filamentous aggregates, also known as amyloids, can propagate their abnormal structures to either the same precursor molecules (seeding) or other protein monomers (cross-seeding). Cross-seeding has been implicated in the abnormal protein aggregation and has been found to facilitate the formation of physiological amyloids. It has risen to be an exciting area of research with a high volume of published reports. In this review article, we focus on the biophysical processes underlying the cross-seeding for some of the most commonly studied amyloid proteins. Here we will discuss the relevant literature related to cross-seeded polymerization of amyloid-beta, human islet amyloid polypeptide (hIAPP, or also known as amylin) and alpha-synuclein. SEVI (semen-derived enhancer of viral infection) amyloid formation by the cross-seeding between the bacterial curli protein and PAP_248-286 is also briefly discussed.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

MeSH terms

Amyloid / chemistry*
Biophysical Phenomena*
Humans
Protein Aggregates*

Substances

Amyloid
Protein Aggregates

Abstract

Publication types

MeSH terms

Substances

Grants and funding