Interaction studies of coumaroyltyramine with human serum albumin and its biological importance
| Autor: | Babu Sudhamalla, Rajagopal Subramanyam, Satyabala Neelam, Mahesh Gokara, Damu G. Amooru |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Circular dichroism Coumaric Acids Physalis Stereochemistry Serum albumin Fluorescence Hydrophobic effect Materials Chemistry medicine Humans Physical and Theoretical Chemistry Binding site Protein secondary structure Serum Albumin biology Chemistry Circular Dichroism Human serum albumin Ligand (biochemistry) Binding constant Surfaces Coatings and Films body regions biology.protein Thermodynamics medicine.drug |
| Zdroj: | The journal of physical chemistry. B. 114(8) |
| ISSN: | 1520-5207 |
| Popis: | N-trans-p-coumaroyltyramine (CT) isolated from Physalis minima is a phenolic substance exhibiting many pharmacological activities like potent inhibition of acetyl cholinesterase, cell proliferation, platelet aggregation, and also antioxidant activity. Here, we have studied the binding of CT with HSA at physiological pH 7.2 by using fluorescence, circular dichroism spectroscopy, mass spectrometry, and molecular docking methods. From the fluorescence emission studies, the number of binding sites and binding constant were calculated to be 2 and (4.5 +/- 0.01) x 10(5) M(-1), respectively. The free energy change was calculated as -7.6 kcal M(-1) at 25 degrees C, which indicates the hydrophobic interactions of CT with HSA and is in well agreement with the computational calculations and molecular docking studies. The changes in the secondary structure of HSA after its complexation with the ligand were studied with CD spectroscopy, which indicated that the protein became partially unfolded. Also, temperature did not affect the HSA-CT complexes. The binding of CT with HSA was detected as 2 molecules bound to HSA was determined using micro TOF-Q mass spectrometry. Further, molecular docking studies revealed that CT was binding at subdomain IIA with hydrophobic interactions and also by hydrogen-bond interactions between the hydroxyl (OH) group of carbon-16 and carbon-2 of CT and Arg222, Ala291, Val293, and Met298 of HSA, with hydrogen-bond distances of 2.488, 2.811, 2.678, and 2.586 A, respectively. |
| Databáze: | OpenAIRE |
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