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Characterization of Arginine Preventive Effect on Heat-Induced Aggregation of Insulin Publisher Pubmed



Haghighipoodeh S1 ; Kurganov B2 ; Navidpour L3 ; Yaghmaei P1 ; Ebrahimhabibi A4, 5
Authors
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Authors Affiliations
  1. 1. Department of Biology, Faculty of Basic Sciences, Science and Research Branch, Islamic Azad University, Tehran, Iran
  2. 2. Department of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology� of the Russian Academy of Sciences, Leninsky pr. 33, Moscow, 119071, Russian Federation
  3. 3. Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 14174, Iran
  4. 4. Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Jalal-al-Ahmad Street, Chamran Highway, Tehran, 1411713137, Iran
  5. 5. Endocrinology and Metabolism Molecular-Cellular Sciences Institute, Tehran University of Medical Sciences, Iran

Source: International Journal of Biological Macromolecules Published:2020


Abstract

Aggregation of proteins can affect their efficacy, and is especially important concerning therapeutic proteins such as insulin. Use of additives such as amino acids can counteract this deleterious process. Heat-induced aggregate formation of human insulin was kinetically studied with the use of various concentrations of the protein, at different temperatures, and in the presence of EDTA by UV–visible spectrophotometry. Effect of arginine, lysine, and histidine was then tested on the process at pH 4.8 and 45 °C. Kinetic parameters of the obtained growth curves (parameters t* and t0.5 characterizing the rate of the nucleation stage and the rate of the stage of aggregate growth respectively) were computed in all these conditions, and structure of aggregates was characterized by spectrofluorimetry, and transmission electron microscopy (TEM). Presence of high concentrations of the chelator EDTA increased aggregation. Among used additives, L-arginine (50 mM) most efficiently suppresses the heat-induced amorphous aggregation of insulin, affecting parameters t0.5 and t* presumably by preserving the protein's structure, as observed by the protein intrinsic fluorescence and CD spectra, and smaller formed aggregates in TEM images and dynamic light scattering. Docking experiment and subsequent molecular dynamics simulation indicated possible sites of interaction for arginine with the B-chain of insulin. © 2019
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