The benzene metabolite p-benzoquinone inhibits the catalytic activity of bovine liver catalase: A biophysical study

Jena, Atala Bihari; Samal, Rashmi Rekha; Kumari, Kanchan; Pradhan, Jyotsnamayee; Chainy, G.B.N.; Subudhi, Umakanta; Pal, Satyanarayan; Dandapat, Jagnehswar

doi:10.1016/j.ijbiomac.2020.11.044

Cited by 26 publications

(6 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The experimental results suggested that the binding process of NDP to BLC took place via hydrophilic contact and the secondary structure of BLC was changed by NDP. [ 62 ]…”

Section: Resultsmentioning

confidence: 99%

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

View full text Add to dashboard Cite

Nifedipine (NDP), a dihydropyridine calcium antagonist, is widely used for the treatment of hypertension and angina pectoris. Catalase is a key antioxidant enzyme that is closely relevant to the level of reactive oxygen specie in vivo. Here, the research explored the effects of NDP on the conformation and catalytic function of bovine liver catalase (BLC) through enzymatic reaction kinetic techniques, multispectroscopic analysis, and computer simulation methods. Kinetic studies clarified that the NDP reduced the activity of BLC using a noncompetitive inhibition mechanism.Based on trial data, a static quenching mechanism functioned in quenching the intrinsic fluorescence of BLC. The binding constant value was (4.486 ± 0.008) Â 10 4 M À1 (298 K) and BLC had one binding site for NDP. Tyr was prone to be exposed more to a hydrophilic environment in wake of a shift in fluorescence value. The binding reaction of BLC to NDP caused a conformational change in BLC, which in turn led to

show abstract

“…The experimental results suggested that the binding process of NDP to BLC took place via hydrophilic contact and the secondary structure of BLC was changed by NDP. [ 62 ]…”

Section: Resultsmentioning

confidence: 99%

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

View full text Add to dashboard Cite

show abstract

“…In general, proteins become functional after being folded into specific globular structure. During protein folding, hydrophobic amino acids get buried in the core of the protein to get protected from water, leading to the protein fold stable [53,54] . Phe8, Ile152, Phe294, Val297, Val303 hydrophobic Amino acids of M Pro generally interact with 8‐HDS during the 100 ns simulation which caused instability in the protein ( Figure S10 ).…”

Section: Discussionmentioning

confidence: 99%

A Computational Insight on the Inhibitory Potential of 8‐Hydroxydihydrosanguinarine (8‐HDS), a Pyridone Containing Analog of Sanguinarine, against SARS CoV2**

Jena

Kanungo

Chainy

et al. 2022

Chemistry & Biodiversity

View full text Add to dashboard Cite

The unprecedented global pandemic of COVID‐19 has created a daunting scenario urging an immediate generation of therapeutic strategy. Interventions to curb the spread of viral infection primarily include setting targets against the virus. Here in this study we target S protein to obstruct the viral attachment and entry and also the M pro to prevent the viral replication. For this purpose, the interaction of S protein and M pro with phytocompounds, sanguinarine and eugenol, and their derivatives were studied using computational tools. Docking studies gave evidence that 8‐Hydroxydihydrosanguinarine, a derivative of sanguinarine, showed maximum binding affinity with both the targets. The binding energies of the ligand with S protein and M pro scored to be ΔGb ‐9.4 Kcal/mol and ΔGb ‐10.3 Kcal/mol respectively. MD simulation studies depict that the phytocompound could effectively cause structural perturbations in the targets which would affect their functions.8‐Hydroxydihydrosanguinarine distorts the α‐helix in the secondary structure of M pro and RBD site of S protein. Protein‐protein interaction study in presence of 8‐hydroxydihydrosanguinarine (8‐HDS) also corroborate the above findings which indicate that this polyphenol interfere in the coupling of S Protein and ACE2. The alterations in protonation of M pro suggest that the protein structure undergoes significant structural changes at neutral pH. ADME (Physicochemical, Lipophilicity, Water Solubility, Pharmacokinetics, Drug‐likeness) property of 8‐ hydroxydihydrosanguinarine indicates this could be a potential drug. This makes the phyto‐alkaloid a possible therapeutic molecule for antiCOVID‐19 drug design.

show abstract

“…Due to the presence of several functional OH groups, catechin has a high binding a nity for the receptor. It has a higher a nity for all NLRP3 complex proteins due to their chemical characteristics, which include a large amount of OH groups on their surface [32,43]. The higher binding a nity of both antioxidants for the essential NLRP3 protein in their complexes suggests that curcumin and EGCG may impact the complex's function.…”

Section: Discussionmentioning

confidence: 99%

An in silico investigation on the interactions of curcumin and epigallocatechin-3-gallate with NLRP3 Inflammasome complex

Jena

Dash²,

Duttaroy

2022

Preprint

Self Cite

View full text Add to dashboard Cite

Interleukin-1β (IL-1β) and IL-18 are the underlying factors of the inflammatory response and are necessary for the host's reaction and pathogen resistance. These cytokines also promote damage during chronic inflammation along with acute tissue injury. However, little is known about how these proteins are made and secreted from cells. Inflammasomes are multi-protein complexes which are required for the canonical synthesis of IL-1β. The NLRP3 inflammasome complex is one of the most studied inflammasome complexes. Its activation is dependent on two signals, i.e. one "primes" the cells by inducing the production of NLRP3 and pro-IL-1β, while the other causes the complex to assemble and activate. Lysosomal rupture, reactive oxygen species, and cytosolic ion perturbation function as the second signal. Despite extensive research, the exact role and regulation of the NLRP3 inflammasome are still unknown. In the current study, we investigated the inhibitory effect of plant-derived compounds such as curcumin and epigallocatechin-3-gallate (EGCG) on NLRP3-mediated IL-1β and IL-18 production using in silicoapproach. Our data suggest that the therapeutic effect of curcumin and EGCG may be due to the inhibition of inflammasome activation. The molecular and protein-protein interaction data indicated that the therapeutic effects of these two polyphenols are mediated by preventing the development of the NLRP3 complex.

show abstract

The benzene metabolite p-benzoquinone inhibits the catalytic activity of bovine liver catalase: A biophysical study

Cited by 26 publications

References 52 publications

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

A Computational Insight on the Inhibitory Potential of 8‐Hydroxydihydrosanguinarine (8‐HDS), a Pyridone Containing Analog of Sanguinarine, against SARS CoV2**

An in silico investigation on the interactions of curcumin and epigallocatechin-3-gallate with NLRP3 Inflammasome complex

Contact Info

Product

Resources

About