The inhibition of heat-induced beta-lactoglobulin aggregation by axially coordinated Zr phthalocyanines.

Автор(и)

  • S. V. Chernii Institute of Molecular Biology and Genetics NASU
  • I. M. Tretyakova V. I. Vernadskii Institute of General and Inorganic Chemistry NASU
  • R. O. Selin V. I. Vernadskii Institute of General and Inorganic Chemistry NASU
  • M. Yu. Losytskyy Institute of Molecular Biology and Genetics NASU
  • V. Ya. Chernii V. I. Vernadskii Institute of General and Inorganic Chemistry NASU
  • V. B. Kovalska Institute of Molecular Biology and Genetics NASU

Анотація

Formation of the beta-pleated protein aggregates – amyloid fibrils – involve into a group of amyloid‐associated disorders as well as into physiological processes. Moreover, specific proteins found in food sources, particularly beta-lactoglobulin (BLG), are able to aggregate into fibrils under heat treatment. The development of agents that would effectively control aggregation is an active area of research to prevent fibril formation. Phthalocyanine complexes were selected for this aim as they are known as compounds with high anti-prionic and antiamyloidogenic activity.

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Медична та фармацевтична хімія