A comparative study of the binding characteristics of ceftriaxone, cefoperazone and cefsudolin to human serum albumin

IUBMB Life ◽  
1996 ◽  
Vol 40 (4) ◽  
pp. 823-831
Author(s):  
Bibiana Nerli ◽  
Beatriz Farruggia ◽  
Guillermo Picó
Keyword(s):  
Human Serum Albumin ◽  
Comparative Study ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Characteristics

scholarly journals Spectroscopic and molecular docking studies reveal binding characteristics of nazartinib (EGF816) to human serum albumin

2020 ◽  
Vol 7 (1) ◽  
pp. 191595 ◽  
Author(s):  
Abdulrahman A. Almehizia ◽  
Haitham AlRabiah ◽  
Ahmed H. Bakheit ◽  
Eman S. G. Hassan ◽  
Rashed N. Herqash ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Kinase Inhibitor ◽  
Electrostatic Force ◽  
Total Binding Energy ◽  
Serum Albumins ◽  
Binding Characteristics ◽  
Theoretical Approaches ◽  
Anti Cancer

The interactions of novel anti-cancer therapeutic agents with the different plasma and tissue components, specifically serum albumins, have lately gained considerable attention due to the significant influence of such interactions on the pharmacokinetics and/or -dynamics of this important class of therapeutics. Nazartinib (EGF 816; NAZ) is a new anti-cancer candidate proposed as a third-generation epidermal growth factor receptor tyrosine kinase inhibitor that is being developed and clinically tested for the management of non-small cell lung cancer. The current study aimed to characterize the interaction between NAZ and human serum albumin (HSA) using experimental and theoretical approaches. Experimental results of fluorescence quenching of HSA induced by NAZ revealed the development of a statically formed complex between NAZ and HSA. Interpretation of the observed fluorescence data using Stern–Volmer, Lineweaver–Burk and double-log formulae resulted in binding constants for HSA-NAZ complex in the range of (2.34–2.81) × 10 4 M –1 over the studied temperatures. These computed values were further used to elucidate thermodynamic attributes of the interaction, which showed that NAZ spontaneously binds to HSA with a postulated electrostatic force-driven interaction. This was further verified by theoretical examination of the NAZ docking on the HSA surface that revealed an HSA-NAZ complex where NAZ is bound to HSA Sudlow site I driven by hydrogen bonding in addition to electrostatic forces in the form of pi-H bond. The HSA binding pocket for NAZ was shown to encompass ARG 257, ARG 222, LYS 199 and GLU 292 with a total binding energy of −25.59 kJ mol –1 .

scholarly journals Probing the toxic interactions between the reactive dye Drimaren Red and Human Serum Albumin

2021 ◽  
Author(s):  
Thais Meira Menezes ◽  
Caio Rodrigo Dias de Assis ◽  
Antonio Marinho da Silva Neto ◽  
Priscila Gubert ◽  
Marcos Gomes Ghislandi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Textile Industry ◽  
Electrostatic Interactions ◽  
Reactive Dye ◽  
Biological Macromolecules ◽  
Spectroscopic Techniques ◽  
Binding Characteristics

Azo dyes like Drimaren Red CL-5B (DR, CI Reactive Red 241) represent a class of compounds extensively used in the textile industry and are extremely dangerous to the environment and human health. Therefore, understanding the binding characteristics between such substances and biological macromolecules is essential from a toxic-kinetic perspective. The molecular interaction between DR and Human Serum Albumin (HSA) was investigated through spectroscopic techniques and molecular docking approaches. The results indicate that DR quenches HSA fluorescence following a static mechanism (corroborated by UV-Vis studies) with a moderate interaction (Ka~105 M-1), guided by electrostatic interactions (DS> 0 and DH< 0). DR is 5.52 nm distant from fluorophore residue Trp-214 (according to FRET investigations), and the interaction is mainly related to Tyr residues (as revealed by synchronous fluorescence). The Ellman assay identified a decrease in the content of HSA free thiol. The results of the RLS demonstrate that there are HSA alterations, suggesting damage to the confirmation of the protein. Molecular docking suggests the binding site of DR was located in subdomain IIB HSA, corroborating the experimental properties. Finally, the results suggest a high potential for DR toxicity triggered by contact with key proteins, which affects the biomolecule functionalities.

Molecular interaction investigation between three CdTe:Zn 2+ quantum dots and human serum albumin: A comparative study

2015 ◽  
Vol 136 ◽  
pp. 955-962 ◽  
Author(s):  
Shan Huang ◽  
Hangna Qiu ◽  
Yi Liu ◽  
Chusheng Huang ◽  
Jiarong Sheng ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Human Serum Albumin ◽  
Comparative Study ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interaction
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