Encapsulation of testosterone and its aliphatic and aromatic dimers by milk beta-lactoglobulin

International Journal of Biological Macromolecules
P ChanphaiHeidar-Ali Tajmir-Riahi

Abstract

The encapsulation of testosterone and it aliphatic dimer (alip) and aromatic dimer (arom) with milk β-lactoglobulin (β-LG) was studied in aqueous solution at pH 7.4. Multiple spectroscopic methods, transmission electron microscopy (TEM) and molecular modeling were used to characterize testosterone-β-LG binding and protein aggregation process. Spectroscopic analysis showed that steroids bind β-LG via hydrophobic and H-bonding interactions with overall binding constants K test-β-LG = 5.6 (± 0.6) × 10(4)M(-1), K test-dimeralip-β-LG = 4.8 (± 0.5) × 10(3)M(-1) and K test-dimer-arom-β-LG = 2.9 (± 0.4) × 10(4)M(-1). The binding affinity was testosterone > testosterone dimer-aromatic > testosterone dimer-aliphatic. Transmission electron microscopy showed major changes in protein morphology as testosterone-protein complexation occurred with increase in the diameter of the protein aggregate indicating encapsulation of steroids by β-LG. Modeling showed the presence of H-bonding stabilized testosterone-β-LG complexes with the free binding energy of -9.82 Kcal/mol indicating that the interaction process is spontaneous at room temperature.

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Citations

Sep 28, 2015·Journal of Photochemistry and Photobiology. B, Biology·P ChanphaiH A Tajmir-Riahi
Jun 5, 2016·Journal of Photochemistry and Photobiology. B, Biology·P ChanphaiH A Tajmir-Riahi
Aug 14, 2019·Journal of Biomolecular Structure & Dynamics·P ChanphaiH A Tajmir-Riahi
May 1, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Alexis PaquinGervais Bérubé
Jul 12, 2019·International Journal of Biological Macromolecules·P Chanphai, H A Tajmir-Riahi

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