Publication details
Characterization of the binding interaction of anti-malarial alkaloid cryptolepine with HSA under physiological conditions using multi-spectroscopic and molecular docking techniques
| Authors | |
|---|---|
| Year of publication | 2025 |
| Type | Article in Periodical |
| Magazine / Source | CHEMICAL PHYSICS |
| MU Faculty or unit | |
| Citation | |
| web | https://www.sciencedirect.com/science/article/pii/S0301010425002848?via%3Dihub |
| Doi | https://doi.org/10.1016/j.chemphys.2025.112883 |
| Keywords | Human serum albumin; Cryptolepine; Fluorescence quenching; Synchronous fluorescence; FRET; Docking |
| Description | The binding of the alkaloid cryptolepine (CRP) with human serum albumin (HSA) was studied employing different spectroscopic techniques. The order of binding constant was found to be around 104 M- 1 at 25 degrees C and temperature dependence of the binding constant infers the association to be exothermic. CRP quenched the fluorescence intensity of the protein. Studies revealed the mode of quenching to be static in nature. Calculations show that the distance between CRP and tryptophan of HSA was less than 8 nm which is ideal for fluorescence resonance energy transfer (FRET). Theoretical studies reveal that CRP is inserted into the III A subdomain of HSA. Negative value of Delta G degrees infers that the overall process is spontaneous. Results obtained from our studies provide detail insight of the interaction of CRP with HSA and this in turn may lead to better understanding of the distribution of pharmacologically active compounds via blood plasma. |