Effect of Ovocystatin on Amyloid β 1-42 Aggregation-In Vitro Studies.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
12 Mar 2023
Historique:
received: 20 01 2023
revised: 07 03 2023
accepted: 08 03 2023
medline: 30 3 2023
entrez: 29 3 2023
pubmed: 30 3 2023
Statut: epublish

Résumé

Amyloid β peptides (Aβ) aggregating in the brain have a potential neurotoxic effect and are believed to be a major cause of Alzheimer's disease (AD) development. Thus, inhibiting amyloid polypeptide aggregation seems to be a promising approach to the therapy and prevention of this neurodegenerative disease. The research presented here is directed at the determination of the inhibitory activity of ovocystatin, the cysteine protease inhibitor isolated from egg white, on Aβ42 fibril genesis in vitro. Thioflavin-T (ThT) assays, which determine the degree of aggregation of amyloid peptides based on fluorescence measurement, circular dichroism spectroscopy (CD), and transmission electron microscopy (TEM) have been used to assess the inhibition of amyloid fibril formation by ovocystatin. Amyloid beta 42 oligomer toxicity was measured using the MTT test. The results have shown that ovocystatin possesses Aβ42 anti-aggregation activity and inhibits Aβ42 oligomer toxicity in PC12 cells. The results of this work may help in the development of potential substances able to prevent or delay the process of beta-amyloid aggregation-one of the main reasons for Alzheimer's disease.

Identifiants

pubmed: 36982505
pii: ijms24065433
doi: 10.3390/ijms24065433
pmc: PMC10049317
pii:
doi:

Substances chimiques

Amyloid beta-Peptides 0
ovocystatin 0
Peptide Fragments 0
Amyloid 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Ministry of Education and Science in the "Regional Initiative of Excellence" program for the years 2019-2022
ID : 016/RID/2018/19

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Auteurs

Bartłomiej Stańczykiewicz (B)

Division of Consultation Psychiatry and Neuroscience, Department of Psychiatry, Wroclaw Medical University, L. Pasteura 10, 50-367 Wroclaw, Poland.

Tomasz M Goszczyński (TM)

Department of Experimental Oncology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, R. Weigla 12, 53-114 Wroclaw, Poland.

Paweł Migdał (P)

Department of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

Marta Piksa (M)

Department of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

Krzysztof Pawlik (K)

Department of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

Jakub Gburek (J)

Department of Pharmaceutical Biochemistry, Division of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211 A, 50-556 Wroclaw, Poland.

Krzysztof Gołąb (K)

Department of Pharmaceutical Biochemistry, Division of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211 A, 50-556 Wroclaw, Poland.

Bogusława Konopska (B)

Department of Pharmaceutical Biochemistry, Division of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211 A, 50-556 Wroclaw, Poland.

Agnieszka Zabłocka (A)

Department of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

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Classifications MeSH