Bin Tang

Bio: Bin Tang is an academic researcher from Sichuan University. The author has contributed to research in topics: Human serum albumin & Docking (molecular). The author has an hindex of 14, co-authored 28 publications receiving 384 citations.

Investigation on the interaction of antibacterial drug moxifloxacin hydrochloride with human serum albumin using multi-spectroscopic approaches, molecular docking and dynamical simulation

Abstract: The interaction between moxifloxacin hydrochloride (MOXH) and human serum albumin (HSA) was experimentally and simulatively investigated. Fluorescence quenching presented that MOXH bound to HSA via a static process, resulting in the formation of MOXH–HSA complex. This quenching mechanism was further verified by time-resolved fluorescence. Binding constants (Ka) of the complex were found to be 105 L mol−1 according to fluorescence data, and the calculated thermodynamic parameters indicated that hydrogen bonds and van der Waals force played key roles in the binding process. The UV-vis absorption, synchronous fluorescence, three-dimensional fluorescence, and circular dichroism spectra suggested that binding with MOXH induced the conformational changes on HSA; the hydrophobicity around tryptophan residues increased, the α-helix content increased, whereas the β-sheet and turn content of HSA decreased. Displacement experiments demonstrated that MOXH mainly bound to site I of HSA. Molecular docking results supported the active site and showed that the diazabicyclo of MOXH inserted into the hydrophobic pocket of HSA. Molecular dynamics simulation further ascertained that MOXH steadily bound to site I of HSA. In conclusion, hydrogen bonds and VDW force played major roles in stabilizing the MOXH–HSA complex, and hydrophobic force was also involved in the binding process.

Characterization of the binding of a novel antitumor drug ibrutinib with human serum albumin: Insights from spectroscopic, calorimetric and docking studies.

Abstract: Ibrutinib (IBR) is a novel Bruton's tyrosine kinase inhibitor and shows good efficacy for several B-cell malignancies. In the current study, the molecular mechanism of the interaction between IBR and the transport protein human serum albumin (HSA) was ascertained by spectroscopic, calorimetric, and docking studies. Detailed investigations on affinity parameter, binding model, conformational change, and site selectivity were implemented by receptor-based and ligand-based analysis. An unusual fluorescence co-quenching (mutual quenching) was observed in the binding of IBR to HSA, followed by a static mechanism. Fluorescence spectroscopy and isothermal titration calorimetry indicated that the binding affinity was at 104 M−1 level and electrostatic interactions and hydrophobic forces contributed the interaction. UV–vis and 3D fluorescence spectroscopy suggested the conformational changes of HSA after binding with IBR. Fourier transform infrared and circular dichroism spectroscopy further verified the variation in the secondary structure of HSA. Site-markers competition and molecular docking confirmed that IBR preferably binds to HSA at the cysteine-rich region of Sudlow's site I (subdomain IIA). This study systematically clarified the binding process of the novel antitumor drug with the functional biomacromolecule for the first time. The findings are helpful for IBR pharmacological assessment and can provide valuable reference for other tinib-type drugs.

I and i

Abstract: There is, I think, something ethereal about i —the square root of minus one. I remember first hearing about it at school. It seemed an odd beast at that time—an intruder hovering on the edge of reality. Usually familiarity dulls this sense of the bizarre, but in the case of i it was the reverse: over the years the sense of its surreal nature intensified. It seemed that it was impossible to write mathematics that described the real world in …

Capillary Electrophoresis: Trends and Recent Advances

Abstract: Robert L. C. Voeten,†,‡ Iro K. Ventouri,‡,§ Rob Haselberg,*,† and Govert W. Somsen† †Division of BioAnalytical Chemistry, Department of Chemistry and Pharmaceutical Sciences, Vrije Universiteit Amsterdam, de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands ‡TI-COAST, Science Park 904, 1098 XH Amsterdam, The Netherlands Analytical Chemistry Group, van’t Hoff Institute for Molecular Sciences, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands

Nanoparticle Surface Functionalization: How to Improve Biocompatibility and Cellular Internalization.

Abstract: The use of nanoparticles (NP) in diagnosis and treatment of many human diseases, including cancer, is of increasing interest. However, cytotoxic effects of NPs on cells and the uptake efficiency significantly limit their use in clinical practice. The physico-chemical properties of NPs including surface composition, superficial charge, size and shape are considered the key factors that affect the biocompatibility and uptake efficiency of these nanoplatforms. Thanks to the possibility of modifying physico-chemical properties of NPs, it is possible to improve their biocompatibility and uptake efficiency through the functionalization of the NP surface. In this review, we summarize some of the most recent studies in which NP surface modification enhances biocompatibility and uptake. Furthermore, the most used techniques used to assess biocompatibility and uptake are also reported.