Protonation State Insights into the Influence of Biocatalytic Function for Acetylcholinesterase Mediated by Neonicotinoids DOI

Zhi-Cong He,

Tao Zhang, Wei Peng

et al.

Biochemistry, Journal Year: 2025, Volume and Issue: unknown

Published: April 19, 2025

The catalytic efficiency of acetylcholinesterase (AChE) is likely regulated by the protonation states and conformational adaptations its residues. While neonicotinoid insecticides are recognized for impairing AChE function through neurotoxic mechanisms, precise molecular mechanisms governing this inhibition remain poorly characterized. This investigation elucidates how structural variations among neonicotinoids modulate equilibria Glu-202 His-447 in AChE's triad. Comparative analysis reveals that nitro-substituted (imidacloprid, clothianidin) induce more pronounced state transitions compared to their cyano-containing counterparts (thiacloprid, acetamiprid). Specifically, strong electron-withdrawing nitro groups facilitate conversion from deprotonation (GLU) (GLH) δ- (HID) ε-position (HIE) enhanced electrostatic interactions. These electronic perturbations trigger reorganization within active site, evidenced group-directed residue realignment subsequent H-bond formation. Energy decomposition identifies contributions as primary determinant binding affinity differences, with nitro-neonicotinoids exhibiting stronger interactions than cyano-neonicotinoids. QM/MM metadynamics substantial alterations disrupt biocatalytic function, particularly capacity acetylcholine hydrolysis. Finally, SH-SY5Y-based cellular assays show imidacloprid exhibits strongest inhibitory effect on intracellular activity, while thiacloprid acetamiprid weaker effects, aligning computational predictions. study provides insights into protonation-state-induced mediated neonicotinoids, contributing assessment exogenous ligand-induced potential ecological human health risks.

Language: Английский

The Nanozyme Revolution: Enhancing the Performance of Medical Biosensing Platforms DOI Creative Commons
André Shamsabadi, Tabasom Haghighi, Sara Carvalho

et al.

Advanced Materials, Journal Year: 2023, Volume and Issue: 36(10)

Published: April 27, 2023

Nanozymes represent a class of nanosized materials that exhibit innate catalytic properties similar to biological enzymes. The unique features these have positioned them as promising candidates for applications in clinical sensing devices, specifically those employed at the point-of-care. They notably found use means amplify signals nanosensor-based platforms and thereby improve sensor detection limits. Recent developments understanding fundamental chemistries underpinning enabled development highly effective nanozymes capable clinically relevant biomarkers limits compete with "gold-standard" techniques. However, there remain considerable hurdles need be overcome before nanozyme-based sensors can utilized platform ready use. An overview current understandings disease diagnostics biosensing unmet challenges must considered prior their translation diagnostic tests is provided.

Language: Английский

Citations

71
Biological pretreatment for algal biomass feedstock for biofuel production DOI
Shashi Bhushan, U. Jayakrishnan,

Bharti Shree

et al.

Journal of environmental chemical engineering, Journal Year: 2023, Volume and Issue: 11(3), P. 109870 - 109870

Published: April 11, 2023

Language: Английский

Citations

67
Proteases immobilized on nanomaterials for biocatalytic, environmental and biomedical applications: Advantages and drawbacks DOI Creative Commons
Muhammad Bilal, Sarmad Ahmad Qamar, Diego Carballares

et al.

Biotechnology Advances, Journal Year: 2023, Volume and Issue: 70, P. 108304 - 108304

Published: Dec. 21, 2023

Proteases have gained significant scientific and industrial interest due to their unique biocatalytic characteristics broad-spectrum applications in different industries. The development of robust nanobiocatalytic systems by attaching proteases onto various nanostructured materials as fascinating novel nanocarriers has demonstrated exceptional performance, substantial stability, ease recyclability over multiple reaction cycles under chemical physical conditions. immobilized on may be much more resistant denaturation caused extreme temperatures or pH values, detergents, organic solvents, other protein denaturants than free enzymes. Immobilized present a lower inhibition. use non-porous the immobilization prevents diffusion steric hindrances during binding substrate active sites enzymes compared porous materials; when using very large solid substrates, orientation enzyme must always adequate. advantages problems nanoparticles will discussed this review. continuous batch reactor operations nanocarrier-immobilized been successfully investigated for variety leather, detergent, biomedical, food, pharmaceutical Information about nanomaterials systematically compiled here. Furthermore, highlighted

Language: Английский

Citations

39
Review of covalent organic frameworks for enzyme immobilization: Strategies, applications, and prospects DOI
Jie Feng, Qingyun Huang, Ce Zhang

et al.

International Journal of Biological Macromolecules, Journal Year: 2023, Volume and Issue: 248, P. 125729 - 125729

Published: July 7, 2023

Language: Английский

Citations

38
Glutaraldehyde modification of lipases immobilized on octyl agarose beads: Roles of the support enzyme loading and chemical amination of the enzyme on the final enzyme features DOI Creative Commons
Pedro Abellanas-Pérez, Diego Carballares, Roberto Fernandéz‐Lafuente

et al.

International Journal of Biological Macromolecules, Journal Year: 2023, Volume and Issue: 248, P. 125853 - 125853

Published: July 17, 2023

Lipase B from Candida antarctica (CALB) and lipase Thermomyces lanuginosus (TLL) have been immobilized on octyl agarose at low loading a exceeding the maximum support capacity. Then, enzymes treated with glutaraldehyde inactivated pH 7 in Tris-HCl, sodium phosphate HEPES, giving different stabilities. Stabilization (depending buffer) of highly loaded biocatalysts was found, very likely as consequence detected intermolecular crosslinkings. This did not occur for lowly biocatalysts. Next, were chemically aminated then glutaraldehyde. In case TLL, intramolecular crosslinkings (visible by apparent reduction protein size) increased enzyme stability biocatalysts, an effect that further due to Using CALB, less intense, stabilization lower, even though quite intense biocatalyst. The depended inactivation buffer. interactions between inactivating buffer effects chemical modifications suggest modification studies must be performed under target conditions.

Language: Английский

Citations

24
Efficient and feasible biocatalysts: Strategies for enzyme improvement. A review DOI
Samah Hashim Albayati,

Nima Ghahremani Nezhad,

Abdulrahman M Taki

et al.

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: 276, P. 133978 - 133978

Published: July 20, 2024

Language: Английский

Citations

11
Evaluating Enzymatic Productivity—The Missing Link to Enzyme Utility DOI Open Access
Khawar Sohail Siddiqui, Haluk Ertan, Anne Poljak

et al.

International Journal of Molecular Sciences, Journal Year: 2022, Volume and Issue: 23(13), P. 6908 - 6908

Published: June 21, 2022

Kinetic productivity analysis is critical to the characterization of enzyme catalytic performance and capacity. However, has been largely overlooked in published literature. Less than 0.01% studies which report on present analysis, despite fact that this only measurement method provides a reliable indicator potential commercial utility. Here, we argue reporting data involving native, modified, immobilized enzymes under different reaction conditions will be immense value optimizing enzymatic processes, with view accelerating biotechnological applications. With use examples from wide-ranging studies, demonstrate measure importance translational processes employ them. We conclude review by suggesting steps maximize catalyzed reactions.

Language: Английский

Citations

33
Non-canonical amino acids as a tool for the thermal stabilization of enzymes DOI Creative Commons

Tim Lugtenburg,

Alejandro Gran‐Scheuch, Ivana Drienovská

et al.

Protein Engineering Design and Selection, Journal Year: 2023, Volume and Issue: 36

Published: Jan. 1, 2023

Abstract Biocatalysis has become a powerful alternative for green chemistry. Expanding the range of amino acids used in protein biosynthesis can improve industrially appealing properties such as enantioselectivity, activity and stability. This review will specifically delve into thermal stability improvements that non-canonical (ncAAs) confer to enzymes. Methods achieve this end, use halogenated ncAAs, selective immobilization rational design, be discussed. Additionally, specific enzyme design considerations using ncAAs are discussed along with benefits limitations various approaches available enhance

Language: Английский

Citations

21
Biocatalytic Functionalities of Lignin Peroxidase-Based Systems in Lignin Depolymerization and Pollutants Removal from Environmental Matrices DOI Creative Commons

Anil Kumar Singh,

Roberto Fernandéz‐Lafuente, Jens Ejbye Schmidt

et al.

Current Pollution Reports, Journal Year: 2024, Volume and Issue: 10(3), P. 345 - 361

Published: April 29, 2024

Abstract Purpose of Review In the presented review, we have summarized and highlighted recent developments in use lignin peroxidase (LiP) to remove a variety pollutants from water matrices. The high redox potential LiP is underlined by its excellent catalytic functionalities elimination pharmaceuticals, phenolics, dyes, polycyclic aromatic hydrocarbons (PAHs), endocrine-disrupting chemicals (EDCs), other miscellaneous pollutants. LiP-based computational frameworks for theoretical bioremediation multiple also been discussed, which prompted rise scientific interest. Recent Findings According current studies, both free immobilized LiPs are biocatalysts capable efficient pollutant degradation LMW transformation. Some preparations demonstrated recyclability, enabling reusability cycles. Additionally, degradability makes it easier comprehend mechanisms underlying recalcitrant Summary capacity cleave C–C C–O–C bonds has led widespread application as biocatalyst. Its outstanding catalyze oxidative cleavage effectively used remediation without needing mediators. Nevertheless, brought attention system framework, generated significant

Language: Английский

Citations

8
Biosynthesis of alkanes/alkenes from fatty acids or derivatives (triacylglycerols or fatty aldehydes) DOI Creative Commons
Rodolpho R. C. Monteiro,

Silvia S.O. da Silva,

Célio L. Cavalcante

et al.

Biotechnology Advances, Journal Year: 2022, Volume and Issue: 61, P. 108045 - 108045

Published: Sept. 29, 2022

This review summarizes the most relevant advances in biological transformation of fatty acids (or derivatives) into hydrocarbons to be used as biofuels (biogasoline, green diesel and jet biofuel). Among enzymes, acid decarboxylase from Jeotgalicoccus sp. ATCC 8456 (OleTJE) stands out a promising enzyme. OleTJE may coupled cascade reactions with metalloenzymes or reductases Old Yellow Enzymes (OYE) family perform hydrogenation α-olefins paraffins. The photodecarboxylase Chlorella variabilis NC64A (CvFAP) is an example coupling biocatalysis photocatalysis produce alkanes. Besides (photo)decarboxylation free and/or triacyclglycerols alkanes/alkenes, by enzymes has also been employed. cyanobacterial aldehyde decarbonylase (cAD) Nostoc punctiforme outstanding this kind Overall, these kinds open up new possibilities production renewable sources, even if they have many limitations on current situation. improving features via immobilization coimmobilization, well utilization whole cells haves reviewed.

Language: Английский

Citations

24