Protein Triad Comprising Genetically Fused Hemoglobin and Human Serum Albumins as an Artificial O2 Carrier Resistant to Haptoglobin Binding

2021 ◽  
Author(s):  
Yoshitsugu Morita ◽  
Yuki Shindo ◽  
Teruyuki Komatsu
Keyword(s):  
Human Serum ◽  
Serum Albumins

Serum Albumins Guided Plasmonic Nanoassemblies with Opposite Chiralities

Soft Matter ◽  
2021 ◽  
Author(s):  
Zhaoyi Wang ◽  
Ningning Zhang ◽  
Jincheng Li ◽  
Jun Lu ◽  
Li Zhao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Great Promise ◽  
Plasmonic Nanostructures ◽  
Serum Albumins ◽  
Catalytic Applications

Chiral assemblies by combining natural biomolecules with plasmonic nanostructures hold great promise for plasmonic enhanced sensing, imaging, and catalytic applications. Herein, we demonstrate that human serum albumin (HSA) and porcine...

Chiral recognition and supramolecular photoreaction of 1,1′-binaphthol with bovine and human serum albumins

2012 ◽  
Vol 39 (1) ◽  
pp. 371-383 ◽  
Author(s):  
Masaki Nishijima ◽  
Jae-Won Chang ◽  
Cheng Yang ◽  
Gaku Fukuhara ◽  
Tadashi Mori ◽  
...  
Keyword(s):  
Human Serum ◽  
Chiral Recognition ◽  
Serum Albumins

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 .

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