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Protein–Ligand Interactions, 2nd Edition

A Special Issue of Molecules (ISSN 1420-3049) belonging to the section "Chemical Biology".

Deadline for manuscript submissions: 30 April 2027 | Viewed by 2663

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: spectroscopy, ligand-protein interactions; calorimetry
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

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Keywords

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

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Published Papers (2 papers)

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Research

22 pages, 4149 KB  
Article
Human Serum Albumin Nanoparticles as 3,6-Diazaphenothiazine Delivery System: Preparation and Interaction Studies
by Karolina Kulig, Aleksandra Owczarzy, Patrycja Sarkowicz, Patrycja Piśla, Katarzyna Piordas, Emilia Martula, Małgorzata Jeleń, Beata Morak-Młodawska, Magdalena Ziąbka, Wojciech Rogóż and Małgorzata Maciążek-Jurczyk
Molecules 2026, 31(14), 2541; https://doi.org/10.3390/molecules31142541 - 22 Jul 2026
Viewed by 1135
Abstract
Plasma proteins are becoming more and more popular among researchers due to their minimal toxicity and immunogenicity. The largest percentage of plasma proteins is human serum albumin (HSA). HSA is widely used as a drug carrier due to its biocompatibility and specific affinity [...] Read more.
Plasma proteins are becoming more and more popular among researchers due to their minimal toxicity and immunogenicity. The largest percentage of plasma proteins is human serum albumin (HSA). HSA is widely used as a drug carrier due to its biocompatibility and specific affinity to cancer cells. 10H-3,6-diazaphenothiazine (DAPT) is a newly synthesized phenothiazine derivative with promising anticancer activity. The main aim of this study was to encapsulate the DAPT into human serum albumin nanoparticles (DAPT-HSA-NPs) as well as to study DAPT interaction with HSA based on spectroscopic, microscopic, and calorimetric techniques. HSA nanoparticles with DAPT (DAPT-HSA-NPs) were prepared using the desolvation method, and this reaction was accompanied by a thermal transition. High encapsulation efficiency of DAPT into the HSA-NPs (DAPT-HSA-NPs) was obtained (~100%) and its release kinetics from the DAPT-HSA-NP system followed the zero-order kinetic model. Both nanoparticle preparation (HSA-NPs) and HSA interaction with DAPT (DAPT-HSA) resulted in changes in the HSA secondary structure. Moreover, the process of DAPT binding to HSA was exothermic (ΔH [kcal·mol−1] < 0), and DAPT probably formed a static complex with HSA (kq [L·mol−1·s−1] > 1012) with moderate affinity (Ka [L·mol−1] of the order of 104). Despite reports on human serum albumin nanoparticles (HSA-NPs) and 10H-3,6-diazaphenothiazine (DAPT), no studies on DAPT encapsulation into HSA-NPs have been published. Therefore, HSA-NPs as a 3,6-diazaphenothiazine delivery system, including preparation methods and interaction analysis, have been evaluated. Full article
(This article belongs to the Special Issue Protein–Ligand Interactions, 2nd Edition)
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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 926
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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