Milk caseins as useful vehicle for delivery of dipyridamole drug

Journal of Biomolecular Structure & Dynamics
Hamid DezhampanahLeila Hasani

Abstract

The interaction of bovine milk α- and β-caseins as an efficient drug carrier system with Dipyridamole (DIP) was investigated using spectroscopy and molecular docking studies at different temperatures (20-37 °C). FTIR, CD, and fluorescence spectroscopy methods demonstrated that α- and β-caseins interact with DIP molecule mainly via hydrophobic and hydrophilic interactions and change in secondary structure of α- and β-caseins. DIP showed a higher quenching efficiency and binding constant of α-casein than β-casein. There was only one binding site for DIP and it was located on the surface of the protein molecule. The thermodynamic parameters of calculation showed that the binding process occurs spontaneously and demonstrated that α- and β-caseins provide very good binding and entrapment to DIP via hydrogen bonds, Van der Waals forces, and hydrophobic interactions. Fluorescence resonance energy transfer, synchronous fluorescence spectroscopy, and docking study showed that DIP binds to the Trp residues of α- and β-casein molecules with short distances. Docking study showed that DIP molecule made several hydrogen bonds and van der Waals interactions with α- and β-caseins. The study of cell culture and micellar solubility of DIP demons...Continue Reading

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Citations

Jan 29, 2020·Journal of Biomolecular Structure & Dynamics·Masoomeh EsmailiMahvash Hadavi
May 30, 2020·Journal of Biomolecular Structure & Dynamics·Shiwani Rana, Kalyan Sundar Ghosh
Jun 30, 2019·Journal of Biomolecular Structure & Dynamics·Nassim Fattahian KalhorAli Akbar Saboury
May 6, 2021·Luminescence : the Journal of Biological and Chemical Luminescence·Yanzhou TaoLi Li

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Methods Mentioned

BETA
coronary bypass
circular dichroism
ELISA
infrared spectroscopy
FRET
Fluorescence
fluorescence resonance
fluorescence resonance energy transfer
fluorescence spectroscopy

Software Mentioned

SWISS
Autodock
Promod
MODEL
CDNN

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