Proteins and Enzymes Applications in Medical, Pharmaceutical and Industrial Biocatalysis Processes

A special issue of Processes (ISSN 2227-9717). This special issue belongs to the section "Pharmaceutical Processes".

Deadline for manuscript submissions: closed (25 March 2023)

Special Issue Editors


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Guest Editor
Department of Biomedical Sciences, College of Veterinary Medicine, King Faisal University, Al-Ahsa 31982, Saudi Arabia
Interests: enzymology; drug discovery; enzyme inhibitors; chemotherapy; bioinformatics; chemical biology

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Guest Editor
Department of Pharmacology, Faculty of Medicine, Minia University, El-Minia 61511, Egypt
Interests: pharmacology; drug discovery; enzyme inhibitor

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Guest Editor
Department of Biotechnology and Food Science, Faculty of Applied Sciences, Durban University of Technology, Durban 4000, South Africa
Interests: drug discovery; organic synthesis; analytical techniques; biologically active molecules

Special Issue Information

Dear Colleagues,

Enzymes are gaining prominence for their applications in a wide range of fields, including medicine, pharmacy, animal sciences and industry. Enzyme inhibitors are a vast family of commercially available FDA-approved medications. Enzymes are promising targets for usage in all engineering settings due to their commercial applicability. In recent years, enzymes constituted an important target for pharmaceuticals and biologicals development. This Special Issue will focus on recent developments in enzyme engineering, activity, catalysis and inhibition. Complex interactions with biological systems, as well as the resolution of current and emerging issues, are highly considered in this issue. This Special Issue will serve as a fresh arena for discussing recent breakthroughs in the use of enzymes in crucial sectors such as pharmaceuticals, diseases and industrial processes. We seek full research papers, communications, methodological articles and review articles that emphasize the topic's broad reach.

Topics include but are not limited to:

  • The drug discovery of new enzyme inhibitors;
  • Bioprocess engineering and biocatalysts;
  • The extraction, purification, and evaluation of mutant enzymes;
  • The design, chemical synthesis, optimization and development of new enzyme ligands;
  • Industrial applications of enzymes;
  • Pharmaceutical and medical applications of enzymes and their inhibitors;
  • Molecular machines and robotics based on enzymes mediators;
  • Artificial enzymes and their applications;
  • Computational studies for enzyme activity and the development of inhibitors.

Dr. Mahmoud Kandeel
Dr. Mohamed Aly Morsy
Dr. Katharigatta Narayanaswamy Venugopala
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Processes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2400 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • enzyme catalysis
  • enzyme inhibitors
  • bioprocess engineering
  • industrial biocatalysts
  • biotransformation
  • enzymatic methods
  • drug targets

Published Papers (2 papers)

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Research

13 pages, 2939 KiB  
Article
Synthesis and Characterization of Nanoformulation of the Broad-Spectrum Enzyme Inhibitor Mancozeb by Polyethylene Glycol Capping and Its Dissipation Kinetics in Water Using TiO2 Nanoparticles
by Wafa Mahmoud Daqa, Adil Alshoaibi, Faheem Ahmed and Tentu Nageswara Rao
Processes 2022, 10(12), 2733; https://doi.org/10.3390/pr10122733 - 18 Dec 2022
Cited by 1 | Viewed by 1475
Abstract
The poly(ethylene) glycol (PEG) capped mancozeb nanoformulation was prepared by the ultrasonic method using a 1% mancozeb solution and 20% capping agent, PEG-4000. The synthesized nanoformulation was characterized using UV-visible, FTIR, SEM and TEM techniques. The photolytic and photo catalytic experiments were carried [...] Read more.
The poly(ethylene) glycol (PEG) capped mancozeb nanoformulation was prepared by the ultrasonic method using a 1% mancozeb solution and 20% capping agent, PEG-4000. The synthesized nanoformulation was characterized using UV-visible, FTIR, SEM and TEM techniques. The photolytic and photo catalytic experiments were carried out in a Borosil glass bottle in the presence of sunlight, varying the pH proportions at a single fortification level (1.0 g/mL) in ground water, under sunlight. The optimal catalyst concentration for complete degradation was observed to be 0.1 percent. The mancozeb nanoformulation in water was determined using the HPLC-PDA method, and the rate constant and the 50% degradation (DT50) values were calculated based on the results. The photolytic results show that there is no significant loss of residues due to adsorption. Titanium dioxide (TiO2) was discovered to be an excellent decontaminating catalyst in a variety of water samples. The compound survives for several days in the absence of a catalyst. Full article
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10 pages, 1924 KiB  
Article
The Broad-Spectrum Antitrypanosomal Inhibitory Efficiency of the Antimetabolite/Anticancer Drug Raltitrexed
by Mahmoud Kandeel and Keisuke Suganuma
Processes 2022, 10(11), 2158; https://doi.org/10.3390/pr10112158 - 22 Oct 2022
Cited by 1 | Viewed by 1412
Abstract
Raltitrexed is a classical antifolate drug with antimetabolite and anticancer properties. In this research, we provide its detailed antitrypanosomal inhibition against six Trypanosoma species and investigate its potential mode of action. Molecular dynamics (MD) simulations and in silico analyses were used to track [...] Read more.
Raltitrexed is a classical antifolate drug with antimetabolite and anticancer properties. In this research, we provide its detailed antitrypanosomal inhibition against six Trypanosoma species and investigate its potential mode of action. Molecular dynamics (MD) simulations and in silico analyses were used to track the binding strength and stability. Raltitrexed showed broad-spectrum trypanocidal actions against Trypanosoma brucei brucei GUTat3.1, T. b. rhodesiense IL1501, T. b. gambiense IL1922, T. evansi Tansui, T. equiperdum IVM-t1 and T. congolense IL3000. The estimated IC50 was found to be in the range of 5.18–24.13 µg/mL, indicating inhibition of Trypanosoma in the low micromolar range. Although the co-crystallized ligand had robust hydrogen bonding and lipophilic characteristics, its docking score was only −4.6 compared to raltitrexed’s −7.78, indicating strong binding with T. brucei dihydrofolate reductase-thymidylate synthase (TbDHFR-TS). MD simulations support the strong binding of raltitrexed with TbDHFR-TS evidenced by low root mean square deviation (RMSD), low residues fluctuations, a tight radius of gyration (ROG) and an average of 3.38 ± 1.3 hydrogen bonds during 50 ns MD simulation. The prospective extended spectrum of raltitrexed against Trypanosoma species grants further research for the synthesis of raltitrexed derivatives and repurposing against other protozoa. Full article
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