Biological Evaluation and Interaction of a Newly Designed Anti-cancer Pd(II) Complex and Human Serum Albumin

2011 ◽  
Vol 29 (2) ◽  
pp. 283-296 ◽  
Author(s):  
Adeleh Divsalar ◽  
Ali Akbar Saboury ◽  
Leila Ahadi ◽  
Elham Zemanatiyar ◽  
Hassan Mansouri-Torshizi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Biological Evaluation ◽  
Anti Cancer

Berberine azoles as antimicrobial agents: synthesis, biological evaluation and their interactions with human serum albumin

MedChemComm ◽  
2013 ◽  
Vol 4 (5) ◽  
pp. 839 ◽  
Author(s):  
Shao-Lin Zhang ◽  
Juan-Juan Chang ◽  
Guri L. V. Damu ◽  
Rong-Xia Geng ◽  
Cheng-He Zhou
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Antimicrobial Agents ◽  
Biological Evaluation

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 .

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH3)2Cl2(O2CCH2CH2COOH)-(OCONHC16H33)] with serum albumin – thermodynamic and conformational investigations

2015 ◽  
Vol 39 (12) ◽  
pp. 9234-9241 ◽  
Author(s):  
Li Qi ◽  
Zhong Lu ◽  
Wen-hua Lang ◽  
Lu Guo ◽  
Chang-geng Ma ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Activity ◽  
Binding Properties ◽  
Anti Cancer

A potential anti-cancer compound with high activity was synthesized and its binding properties with human serum albumin were tested.

Probing the Interaction of Anti-Cancer Agent Dihydromyricetin with Human Serum Albumin: A typical Method Study

2012 ◽  
Vol 12 (8) ◽  
pp. 919-928 ◽  
Author(s):  
Tingting Chen ◽  
Shajun Zhu ◽  
Yapeng Lu ◽  
Hui Cao ◽  
Yu Zhao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Anti Cancer ◽  
Cancer Agent ◽  
Typical Method

scholarly journals Doxorubicin-loaded human serum albumin nanoparticles overcome transporter-mediated drug resistance

2019 ◽  
Author(s):  
Hannah Onafuye ◽  
Sebastian Pieper ◽  
Dennis Mulac ◽  
Jindrich Cinatl ◽  
Mark N. Wass ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Neuroblastoma Cell ◽  
Resistance Mechanisms ◽  
Neuroblastoma Cell Line ◽  
Cancer Therapies ◽  
Body Distribution ◽  
Anti Cancer ◽  
Systemic Drug

AbstractResistance to systemic drug therapies is a major reason for the failure of anti-cancer therapies. Here, we tested doxorubicin-loaded human serum albumin (HSA) nanoparticles in the neuroblastoma cell line UKF-NB-3 and its ABCB1-expressing sublines adapted to vincristine (UKF-NB-3rVCR1) and doxorubicin (UKF-NB-3rDOX20). Doxorubicin-loaded nanoparticles displayed increased anti-cancer activity in UKF-NB-3rVCR1and UKF-NB-3rDOX20cells relative to doxorubicin solution, but not in UKF-NB-3 cells. UKF-NB-3rVCR1cells were resensitised by nanoparticle-encapsulated doxorubicin to the level of UKF-NB-3 cells. UKF-NB-3rDOX20cells displayed a more pronounced resistance phenotype than UKF-NB-3rVCR1cells and were not re-sensitised by doxorubicin-loaded nanoparticles to the level of parental cells. ABCB1 inhibition using zosuquidar resulted in similar effects like nanoparticle incorporation, indicating that doxorubicin-loaded nanoparticles circumvent ABCB1-mediated drug efflux. The limited re-sensitisation of UKF-NB-3rDOX20cells to doxorubicin by circumvention of ABCB1-mediated efflux is probably due to the presence of multiple doxorubicin resistance mechanisms. So far, ABCB1 inhibitors have failed in clinical trials, probably because systemic ABCB1 inhibition results in a modified body distribution of its many substrates including drugs, xenobiotics, and other molecules. HSA nanoparticles may provide an alternative, more specific way to overcome transporter-mediated resistance.

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