Analysis of the Amyloid-like Properties of COL2A1 Protein

first_page Download PDF settings Order Article Reprints Font Type: Arial Georgia Verdana Font Size: Aa Aa Aa Line Spacing:    Column Width:    Background: Open AccessAbstract Analysis of the Amyloid-like Properties of COL2A1 Protein † by Aleksandra BrukkelAleksandra Brukkel SciProfiles Scilit Preprints.org Google Scholar 1,*, Andrew A. ZelinskyAndrew A. Zelinsky SciProfiles Scilit Preprints.org Google Scholar 2, Marina V. RyabininaMarina V. Ryabinina SciProfiles Scilit Preprints.org Google Scholar 2 and Aleksandr A. RubelAleksandr A. Rubel SciProfiles Scilit Preprints.org Google Scholar 2 1 SCAMT Institute, ITMO University, 191002 Saint-Petersburg, Russia 2 Laboratory of Amyloid Biology, Saint-Petersburg State University, 199034 Saint-Petersburg, Russia * Author to whom correspondence should be addressed. † Presented at the 3rd International Electronic Conference on Biomolecules, 23–25 April 2024; Available online: https://sciforum.net/event/IECBM2024. Proceedings 2024, 103(1), 80; https://doi.org/10.3390/proceedings2024103080 Published: 12 April 2024 (This article belongs to the Proceedings of The 3rd International Electronic Conference on Biomolecules) Download keyboard_arrow_down Download PDF Download PDF with Cover Download XML Download Epub Versions Notes Keywords: amyloids; collagen type II; yeast test-system; C-DAG test system; protein analysis; protein screening Amyloids are proteins which exist in the form of insoluble aggregates and possess a characteristic cross-beta structure. The formation of amyloid aggregates can be seen during several pathological processes in humans, including neurodegenerative diseases, diabetes, and systemic amyloidoses. Despite their infamous association with the previously mentioned conditions, amyloids can also serve a functional role in biological systems. For example, Pmel17, which is involved in melanin polymerization in mammalian cells, resembles an amyloid structure, and some peptide hormones are also known to be stored in amyloid form in secretory granules of the endocrine system [1]. Thus, studying amyloids as functional proteins may aid in both determining targets for the treatment of pathological conditions and in understanding their unique role in the organism. The analysis of amyloid-like properties requires a comprehensive approach using bioinformatic prediction, which can later be verified using bacterial and yeast systems as well as various biochemical tests. The object of this study is the protein COL2A1, better known as type II collagen. This type of collagen forms the basis of cartilage tissue and its mutant form can cause diseases known as collagenopathies. This protein possesses some distinctive features characteristic of amyloids. These features include Congo red staining and a tendency to form fibrillar structures. In addition, the possibility of it forming amyloid structures was predicted for the third isoform of type II collagen via the ArchCandy program. In this work, we present data on the investigation of COL2A1's amyloid properties in a C-DAG system [2] and a yeast model [3]. Currently, additional studies are being conducted to obtain the protein in a bacterial system to assess its biochemical properties. Author ContributionsConceptualization A.A.R.; data acquisition and formal analysis, A.B., A.A.Z. and M.V.R.; supervision, A.A.R., funding acquisition, A.A.R., writing—review and editing, A.B. and A.A.R. All authors have read and agreed to the published version of the manuscript.FundingThis research was supported by St. Petersburg State University (project No. 95444727).Institutional Review Board StatementNot applicable.Informed Consent StatementNot applicable.Data Availability StatementNot applicable.Conflicts of InterestThe authors declare no conflict of interest.ReferencesRubel, M.S.; Fedotov, S.A.; Grizel, A.V.; Sopova, J.V.; Malikova, O.A.; Chernoff, Y.O.; Rubel, A.A. Functional Mammalian Amyloids and Amyloid-like Proteins. Life 2020, 10, 156. [Google Scholar] [CrossRef] [PubMed]Chandramowlishwaran, P.; Sun, M.; Casey, K.L.; Romanyuk, A.V.; Grizel, A.V.; Sopova, J.V.; Rubel, A.A.; Nussbaum-Krammer, C.; Vorberg, I.M.; Chernoff, Y.O. Mammalian amyloidogenic proteins promote prion nucleation in yeast. J. Biol. Chem. 2018, 293, 3436–3450. [Google Scholar] [CrossRef] [PubMed]Hochschild, S. A bacterial export system for generating extracellular amyloid aggregates. Nat. Protoc. 2013, 8, 1381–1390. [Google Scholar] [CrossRef]Disclaimer/Publisher's Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content. © 2024 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Share and Cite MDPI and ACS Style Brukkel, A.; Zelinsky, A.A.; Ryabinina, M.V.; Rubel, A.A. Analysis of the Amyloid-like Properties of COL2A1 Protein. Proceedings 2024, 103, 80. https://doi.org/10.3390/proceedings2024103080 AMA Style Brukkel A, Zelinsky AA, Ryabinina MV, Rubel AA. Analysis of the Amyloid-like Properties of COL2A1 Protein. Proceedings. 2024; 103(1):80. https://doi.org/10.3390/proceedings2024103080 Chicago/Turabian Style Brukkel, Aleksandra, Andrew A. Zelinsky, Marina V. Ryabinina, and Aleksandr A. Rubel. 2024. "Analysis of the Amyloid-like Properties of COL2A1 Protein" Proceedings 103, no. 1: 80. https://doi.org/10.3390/proceedings2024103080 Article Metrics No No Article Access Statistics Multiple requests from the same IP address are counted as one view.