Journal
RSC ADVANCES
Volume 4, Issue 35, Pages 18205-18216Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3ra46997b
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Funding
- 973 program from the Chinese Ministry of Science and Technology [2012CB720600]
- National Natural Science Foundation of China [21225313]
- Program for Changjiang Scholars, Innovative Research Team in University [IRT1030]
- National Science Foundation of Wuhan University [2042014Kf0287]
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F16 is a novel identified delocalized lipophilic cation (DLC) which has been found to inhibiting a variety of tumor cell proliferation due to its selective accumulation in the mitochondria of carcinoma cells. To gain further insight into the thermodynamic properties of this small molecule, we chose human serum albumin (HSA) as the model protein, and investigated the interactions of F16 and its precursor compound PVI with HSA by comprehensive spectroscopy, electrochemistry and molecule modeling methods. The static fluorescence quenching of HSA suggests that both F16 and PVI can form complexes with HSA, though the binding mechanisms are different. The main driving forces for F16-HSA binding are typical hydrophobic interactions, while PVI-HSA binding takes place through electrostatic interactions. F16-HSA binding shows an adverse temperature dependence recognized as the effect of the high activation energy requirement in the binding process generated by the specific structural obstacle. Both F16 and PVI can bind with HSA and thus benefit their transportation and elimination in body, however, the positive charge of F16 may have negative effect on the binding interaction.
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