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Title: Abundant neuroprotective chaperone Lipocalin-type prostaglandin D synthase (L-PGDS) disassembles the Amyloid-β fbrils
Authors: Kannaian, Bhuvaneswari
Sharma, Bhargy
Phillips, Margaret
Chowdhury, Anup
Manimekalai, Malathy Sony Subramanian
Adav, Sunil Shankar
Ng, Justin Tze Yang
Kumar, Ambrish
Lim, Sierin
Mu, Yuguang
Sze, Siu Kwan
Grüber, Gerhard
Pervushin, Konstantin
Keywords: Science::Biological sciences
Issue Date: 2019
Source: Kannaian, B., Sharma, B., Phillips, M., Chowdhury, A., Manimekalai, M. S. S., Adav, S. S., . . . Pervushin, K. (2019). Abundant neuroprotective chaperone Lipocalin-type prostaglandin D synthase (L-PGDS) disassembles the Amyloid-β fbrils. Scientific Reports, 9(1), 12579-. doi:10.1038/s41598-019-48819-5
Journal: Scientific Reports
Abstract: Misfolding of Amyloid β (Aβ) peptides leads to the formation of extracellular amyloid plaques. Molecular chaperones can facilitate the refolding or degradation of such misfolded proteins. Here, for the first time, we report the unique ability of Lipocalin-type Prostaglandin D synthase (L-PGDS) protein to act as a disaggregase on the pre-formed fibrils of Aβ(1–40), abbreviated as Aβ40, and Aβ(25–35) peptides, in addition to inhibiting the aggregation of Aβ monomers. Furthermore, our proteomics results indicate that L-PGDS can facilitate extraction of several other proteins from the insoluble aggregates extracted from the brain of an Alzheimer’s disease patient. In this study, we have established the mode of binding of L-PGDS with monomeric and fibrillar Aβ using Nuclear Magnetic Resonance (NMR) Spectroscopy, Small Angle X-ray Scattering (SAXS), and Transmission Electron Microscopy (TEM). Our results confirm a direct interaction between L-PGDS and monomeric Aβ40 and Aβ(25–35), thereby inhibiting their spontaneous aggregation. The monomeric unstructured Aβ40 binds to L-PGDS via its C-terminus, while the N-terminus remains free which is observed as a new domain in the L-PGDS-Aβ40 complex model.
ISSN: 2045-2322
DOI: 10.1038/s41598-019-48819-5
Rights: © 2019 The Author(s). Published by Nature Publishing Group. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. Te images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles


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