RESUMO
In the present study, the interaction between Perfluorohexadecanoic acid (PFHxDA) and human serum albumin (HAS) was studied by fluorescence spectroscopy, molecular docking, dynamic simulation and circular dichroism (CD). The interaction character and the effect on human serum albumin conformation were measured by simulating the physiological condition (pH= 7.4). Experiments and simulation results revealed that PFHxDA molecules and HSA have regular fluorescence quenching, and the quenching mechanism is static quenching and non-radiative energy transfer. Thermodynamic analysis revealed the binding behavior was mainly governed by hydrophobic forces. Specific binding site experiments showed that the binding site of PFHxDA was a site I of HSA. The results from the CD spectrum demonstrated that PFHxDA changed the molecular conformation of HSA, which is consistent with the results obtained by molecular docking and dynamic simulation.
RESUMO
@#Surgery has remained the cornerstone of lung cancer therapy. Sleeve lobectomy, which is featured by not only the maximal resection of tumors but also the maximal preservation of functional lung parenchyma, has been proved to be a valid therapeutic option for the treatment of some centrally located lung cancer . Evidence points toward equivalent oncologic outcomes with improved survival and quality of life after sleeve resections compared with pneumonectomy. However, the postoperative morbidities and the long-term results after sleeve lobectomy remain controversial, especially in relation to nodal involvement and after induction therapy. With the development of technology, minimally invasive procedures have been performed more and more widely.