scholarly journals Targeting the Nalidixic Acid Binding Site on Human Serum Albumin Through Computational Approach: A Re-Investigation

2021 ◽  
Vol 12 (2) ◽  
pp. 1520-1525

Nalidixic acid (NA) is a quinolone drug used to treat urinary tract infections. It inhibits bacterial gyrase-DNA complex formation, an essential step for DNA supercoiling during bacterial replication. Due to the medical application of this drug, it would be interesting to get insight into its binding mechanism with human serum albumin (HSA), the primary carrier protein in blood circulation. Two reports of NA binding to HSA were published using molecular docking approaches. The first report revealed that the preferred binding site of NA was Site II of serum albumins, while the recent finding predicted Site I of bovine serum albumin (BSA) as the preferred site. Given the high sequence homology between these albumins, it is presumed that the binding preference of this drug should be the same in these proteins. To re-investigate this phenomenon, the interaction of NA with HSA was conducted using AutoDockTool 4.0. The molecular docking results revealed that NA binding preference was at Site I, involving Lys 199 in HSA, due to the formation of more significant contacts. Hence, it is concluded that any variable or parameters in the software should be wisely standardized to minimize the controversial results using different programs.

RSC Advances ◽  
2016 ◽  
Vol 6 (108) ◽  
pp. 106516-106526 ◽  
Author(s):  
Fereshteh Shiri ◽  
Somaye Shahraki ◽  
Sadegh Baneshi ◽  
Massoud Nejati-Yazdinejad ◽  
Mostafa Heidari Majd

The binding site of new complex Zn(ii) of 5-dithiocarbamato-1,3,4-thiadiazole-2-thiol and HAS.


2020 ◽  
Author(s):  
Nikola Gligorijević ◽  
Vladimir Šukalović ◽  
Goran Miljuš ◽  
Olgica Nedić ◽  
Ana Penezić

ABSTRACTBinding of dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised in detail in this study. Binding process was monitored by spectroscopic methods and molecular docking approach. HSA binds DHLA with moderate affinity, 0.80 ± 0.007 × 104 M−1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Hydrogen bonds and electrostatic interactions were identified as the key binding interactions. DHLA binding thermally stabilized HSA, yet it had no effect on HSA structure and its susceptibility to trypsin digestion. Molecular docking confirmed that Sudlow I site accommodated DHLA in a certain conformation in order for binding to occur. Molecular dynamic simulation showed that formed complex is stable. Reported results offer future perspectives for investigations regarding the use of DHLA as a dietary intervention but also raise concerns about the effectiveness of alpha-lipoic acid and DHLA in treatment of patients with COVID-19.


Soft Matter ◽  
2021 ◽  
Author(s):  
Zhaoyi Wang ◽  
Ningning Zhang ◽  
Jincheng Li ◽  
Jun Lu ◽  
Li Zhao ◽  
...  

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...


Author(s):  
Fahad M. Almutairi ◽  
Mohammad Rehan Ajmal ◽  
Mohammad Khursheed Siddiqi ◽  
Nabeela Majid ◽  
Adel Ibrahim Ahmad Al-Alawy ◽  
...  

2014 ◽  
Vol 41 (4) ◽  
pp. 2377-2387 ◽  
Author(s):  
Manjunath D. Meti ◽  
Kirthi S. Byadagi ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Uttam A. More ◽  
...  

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