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Protein–Ligand Interactions, 2nd Edition

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 15 September 2026 | Viewed by 632

Special Issue Editor


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Guest Editor
Department of Physical Pharmacy, Faculty of Pharmaceutical Sciences in Sosnowiec, Medical University of Silesia in Katowice, Sosnowiec, Poland
Interests: protein-ligand interactions; protein modification
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Interactions between proteins and ligands support the area of biological science. The subject of protein–ligand interactions, especially serum protein, is one of the most exciting subjects in modern science. Due to the physicochemical properties of the studied substances, there are numerous methods and techniques used to analyse their structure–function relationships. Understanding such interactions is crucial to gaining fundamental knowledge related to cellular behavior. The field of protein–ligand interaction studies is at an auspicious developmental stage, as well as being in a very active growth phase. The main goal of this Special Issue is to provide a platform for publishing research on protein–ligand interactions, using useful multi-disciplinary techniques applied in laboratories worldwide to investigate the basic principles and practical applications, especially in the pharmaceutical and biomedical fields.

Prof. Dr. Małgorzata Maciążek-Jurczyk
Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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Keywords

  • protein–ligand interactions
  • binding affinity
  • protein structure and function

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Published Papers (1 paper)

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Research

19 pages, 2387 KB  
Article
Catalase Specifically Binds Antipsychotic Clozapine: Experimental and In Silico Insights into Interactions, Complex Stability, and Dose-Dependent Enzyme Activity Modulation
by Tamara Vasović, Milica Radibratović, Dušan Spasić, Simeon Minić, Čedo Miljević, Nikola Gligorijević and Milan Nikolić
Molecules 2026, 31(8), 1294; https://doi.org/10.3390/molecules31081294 - 16 Apr 2026
Viewed by 378
Abstract
Oxidative stress is intrinsically linked to mental disorders, involving an imbalance between reactive species and antioxidant defenses, where catalase is an essential, ubiquitous antioxidant enzyme. The pleiotropic effects of antipsychotic drugs, used for schizophrenia and mood disorders, are not fully elucidated at the [...] Read more.
Oxidative stress is intrinsically linked to mental disorders, involving an imbalance between reactive species and antioxidant defenses, where catalase is an essential, ubiquitous antioxidant enzyme. The pleiotropic effects of antipsychotic drugs, used for schizophrenia and mood disorders, are not fully elucidated at the molecular level. This study characterized the binding of a highly effective but potentially dangerous antipsychotic, clozapine (CLZ), to commercial bovine liver catalase (BLC). Using various spectroscopic methods under simulated physiological conditions, we found a moderate binding affinity of CLZ for BLC (Ka = 1.4 × 10−5 M−1), subtly influencing the protein’s secondary and tertiary structures and slightly increasing its thermal stability. CLZ efficiently protected BLC against free-radical-induced oxidation and preserved its catalytic activity for decomposing toxic hydrogen peroxide. The effect of CLZ on BLC antioxidant activity was dual: no significant effect at lower, physiologically relevant concentrations, but significant inhibition at saturating, toxic drug concentrations. Molecular docking and molecular dynamics results indicated the presence of two specific binding sites within BLC monomers, one located near its active site. In conclusion, our in vitro results indicate that CLZ’s specific binding to BLC can be both beneficial and potentially harmful, and that this effect is dose-dependent. Full article
(This article belongs to the Special Issue Protein–Ligand Interactions, 2nd Edition)
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