Loading [MathJax]/jax/output/SVG/config.js
Mendeleev Communications
RUS  ENG    JOURNALS   PEOPLE   ORGANISATIONS   CONFERENCES   SEMINARS   VIDEO LIBRARY   PACKAGE AMSBIB  
General information
Latest issue
Archive

Search papers
Search references

RSS
Latest issue
Current issues
Archive issues
What is RSS


Mendeleev Commun.:
Year:
Volume:
Issue:
Page:
Find




Personal entry:
Login:
Password:
Save password
Enter
Forgotten password?
Register

Mendeleev Communications, 2021, Volume 31, Issue 1, Pages 73–75
DOI: https://doi.org/10.1016/j.mencom.2021.01.022 (Mi mendc838) 		 
This article is cited in 2 scientific papers (total in 2 papers)

Communications

Unusual spiral structures formed by glycated β-casein in the presence of thioflavin T: amyloid transformation?

I. A. Zanyatkina, Yu. Yu. Stroylovabc, A. K. Melnikovaa, A. A. Moosavi-Movahedid, A. A. Sabouryd, T. Haertleef, V. I. Muronetzab

a Department of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
b A.N. Belozersky Research Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
c Institute of Molecular Medicine, I.M. Sechenov First Moscow State Medical University, Moscow, Russian Federation
d Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
e Biopolymers, Interactions, Assemblies, UR 1268, Institute National de la Recherche Agronomique, Nantes, France
f Department of Animal Nutrition, Poznan University of Life Sciences, Poznan, Poland
Full-text PDF (373 kB) Citations (2)
DOI: https://doi.org/10.1016/j.mencom.2021.01.022
Abstract: Unusual spiral-like structures in aggregates formed by β-casein glycated in a special way in the presence of thioflavin T are reported. Different glycation agents, temperature, pH, incubation time, and concentrations of protein and modifier were characterized, but only glycated by 200mm glucose for 48h at 37°C without sodium cyanoborohydride β-casein forms spiral structures in the presence of thioflavin T. Thioflavin T affects the size of particles formed by glycated β-casein and also stimulates heat-induced aggregation, indicating that the formation of unusual spiral structures is determined both by the structure of the advanced glycation end products and by the properties of the glycated protein.
Keywords: β-casein, thioflavin T, amyloid structure, aggregation, protein glycation, advanced glycation end-products.
Document Type: Article
Language: English
Supplementary materials:
Supplementary_data_1.pdf (589.7 Kb)


Citation: I. A. Zanyatkin, Yu. Yu. Stroylova, A. K. Melnikova, A. A. Moosavi-Movahedi, A. A. Saboury, T. Haertle, V. I. Muronetz, “Unusual spiral structures formed by glycated β-casein in the presence of thioflavin T: amyloid transformation?”, Mendeleev Commun., 31:1 (2021), 73–75
Linking options:
  • https://www.mathnet.ru/eng/mendc838
  • https://www.mathnet.ru/eng/mendc/v31/i1/p73
    • This publication is cited in the following 2 articles:
    Citing articles in Google Scholar: Russian citations, English citations
    Related articles in Google Scholar: Russian articles, English articles
    		Mendeleev Communications
    Statistics & downloads:
    Abstract page:23
    Full-text PDF :8
     
      Contact us:
    		  Terms of Use  Registration to the website  Logotypes © Steklov Mathematical Institute RAS, 2025