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Protein-Ligand Interactions

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

Deadline for manuscript submissions: 31 December 2024 | Viewed by 1366

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 whole 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 studied substances, there are numerous methods and techniques used in order to analyse their structure–function relationships. Understanding such interactions is crucial for gaining a fundamental knowledge base relating to cellular behaviour. The field of protein–ligand interaction studies is at an auspicious stage of development, 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, by using useful multi-disciplinary techniques applied in laboratories worldwide for investigating the basic principles and practical applications, especially in the pharmaceutical and biomedical fields.

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 (1 paper)

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Research

13 pages, 5173 KiB  
Article
Impact of Transglutaminase-Mediated Crosslinking on the Conformational Changes in a Dual-Protein System and IgE Reactivity of Soy Protein
by Guangliang Xing, Tianran Hui, Jia Liu and Siran Yang
Molecules 2024, 29(14), 3371; https://doi.org/10.3390/molecules29143371 - 18 Jul 2024
Viewed by 798
Abstract
Transglutaminase (TGase)-catalyzed crosslinking has gained substantial traction as a novel strategy for reducing allergenic risk in food proteins, particularly within the realm of hypoallergenic food production. This study explored the impact of TGase crosslinking on conformational changes in a binary protein system composed [...] Read more.
Transglutaminase (TGase)-catalyzed crosslinking has gained substantial traction as a novel strategy for reducing allergenic risk in food proteins, particularly within the realm of hypoallergenic food production. This study explored the impact of TGase crosslinking on conformational changes in a binary protein system composed of soy protein isolate (SPI) and sodium caseinate (SC) at varying mass ratios (10:0, 7:3, 5:5, 3:7 (w/w)). Specifically, the immunoglobulin E (IgE) binding capacity of soy proteins within this system was examined. Prolonged TGase crosslinking (ranging from 0 h to 15 h) resulted in a gradual reduction in IgE reactivity across all SPI-SC ratios, with the order of IgE-binding capability as follows: SPI > SPI5-SC5 > SPI7-SC3 > SPI3-SC7. These alterations in protein conformation following TGase crosslinking, as demonstrated by variable intrinsic fluorescence, altered surface hydrophobicity, increased ultraviolet absorption and reduced free sulfhydryl content, were identified as the underlying causes. Additionally, ionic bonds were found to play a significant role in maintaining the structure of the dual-protein system after crosslinking, with hydrophobic forces and hydrogen bonds serving as supplementary forces. Generally, the dual-protein system may exhibit enhanced efficacy in reducing the allergenicity of soy protein. Full article
(This article belongs to the Special Issue Protein-Ligand Interactions)
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