Review on the delivery of steroids by carrier proteins.
Due to the poor solubility of steroids in aqueous solution, delivery of these biomaterials is of major biomedical importance. We have reviewed the conjugation of testosterone and it aliphatic dimer and aromatic dimer with several carrier proteins, human serum albumin (HSA), bovine serum albumin (BSA) and milk beta-lactoglobulin (b-LG) in aqueous solution at physiological pH. The results of multiple spectroscopic methods, transmission electron microscopy (TEM) and molecular modeling were compared here. Steroid-protein bindings are via hydrophilic and H-bonding contacts. HSA forms more stable conjugate than BSA and b-LG. The stability of steroid-protein conjugates is testosterone>dimer-aromatic>dimer-aliphatic. Encapsulation of steroids by protein is shown by TEM images. Modeling showed the presence of H-bonding, which stabilized testosterone-protein complexes with the free binding energy of -12.95 for HSA and -11.55 for BSA and -8.92kcal/mol for b-LG conjugates. Steroid conjugation induced major perturbations of serum protein conformations. Serum proteins can transport steroids to the target molecules.
Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7, Canada.
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Chanphai
Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7, Canada.
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Vesper
Division of Humanities: Math/Sciences, University of Hawaii-West O'ahu, 1001 Farrington Highway, Kapolei, HI 96707, USA.
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Bariyanga
Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7, Canada.
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Bérubé
Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, Québec G9A 5H7, Canada. Electronic address: tajmirri@uqtr.ca.
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Tajmir-Riahi
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000737:chemistry / Q000378:metabolism; D062105:Molecular Docking Simulation; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared; D013256:Steroids / Q000737:chemistry / Q000378:metabolism*
D002352:Carrier Proteins; D007782:Lactoglobulins; D012709:Serum Albumin; D013256:Steroids; D012710:Serum Albumin, Bovine
Delivery; Modeling; Morphology; Serum protein; TEM; Testosterone