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Mohammad Reza Ashrafi Kooshk

Researcher at Kermanshah University of Medical Sciences

Publications -  7
Citations -  121

Mohammad Reza Ashrafi Kooshk is an academic researcher from Kermanshah University of Medical Sciences. The author has contributed to research in topics: Bovine serum albumin & Albumin. The author has an hindex of 5, co-authored 7 publications receiving 109 citations. Previous affiliations of Mohammad Reza Ashrafi Kooshk include Razi University.

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Comparative Spectroscopic Studies on Curcumin Stabilization by Association to Bovine Serum Albumin and Casein: A Perspective on Drug-Delivery Application

TL;DR: It appears from thermodynamic analyses that in “protein-curcumin” systems, water molecules are excluded from the vicinity of curcumin, so that some of them may provide novel tools to increase both food quality and the bioavailability ofCurcumin as a health promoting agent.
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Protective effects of accompanying proteins on light- and water-mediated degradation of Curcumin

TL;DR: It appears that BSA and casein as protein vehicles are useful tools to increase stability of curcumin, as a health promoting agent.
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Heme-coordinated histidine residues form non-specific functional "ferritin-heme" peroxidase system: Possible and partial mechanistic relevance to oxidative stress-mediated pathology in neurodegenerative diseases.

TL;DR: Peroxidase-/nitrative-mediated oxidation of vital molecules as well as ferritin-induced catalase inhibition using in vitro experimental system is discussed and its contribution as an important causative pathogenesis mechanism in some neurodegenerative disorders is described.

In Vitro Anti-Cancer Activity of Native Curcumin and “Protein-Curcumin” Systems: A Perspective on Drug-Delivery Application

TL;DR: It appears that BSA and casein as protein vehicles are useful tools to increase both food quality and the bioavailability of curcumin as health promoting agent, but results imply that the chemical modification of proteins cannot improve the anti-cancer activity ofCurcumin despite increasing of their binding affinity.