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Commentary Open Access
Volume 4 | Issue 1 | DOI: https://doi.org/10.46439/aging.4.018

Environmental determinants for protein structuring and amyloid transformation

  • 1Department of Bioinformatics and Telemedicine, Jagiellonian University -Medical College, 30-688 Krakow, Medyczna 7 Poland
  • 2Faculty of Automatic, Electronics and Computer Science, Department of Applied Informatics, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland
  • 3ABB Business Services Sp. z o.o. ul. ?ega?ska 1, 04-713 Warszawa, Poland
  • 4Chair of Medical Biochemistry, Jagiellonian University - Medical College, 31-034 Krakow, Kopernika 7, Poland
+ Affiliations - Affiliations

Corresponding Author

Roterman I, myroterm@cyf-kr.edu.pl

Received Date: July 18, 2024

Accepted Date: August 08, 2024

Abstract

Amyloid transformation under laboratory conditions is achieved by shaking an aqueous solution of any protein. The shaking time varies significantly, demonstrating the variable degree of ease of structural transformation in a given protein. The structural specificity that distinguishes amyloid forms from biologically active proteins is the flatness (two-dimensionality) of the form of each chain in the amyloid fibril. The 2D feature, given the globular and therefore 3D structure of biologically active proteins, is an object of analysis in the search for factors favoring amyloid transformation. The use of a modified fuzzy oil drop model (FOD-M) enables this transformation to be mathematically expressed. The mathematical expression is directly related to the shaking conditions, while leaving open the question of an environmental factor under physiological conditions that causes a conformational change resulting in a 2D structure of the polypeptide chain. The examples expressing the environmental prerequisites demonstrated in the current review show the dependence of structuring on the external force field.

Keywords

Amyloid, Transthyretin, VL domain IgG, Synuclein, Enzymes, Hydrophobicity, External force field, Structural changes, Amyloid transformation

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