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Serum Protein-Ligand Interactions

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

Deadline for manuscript submissions: closed (30 November 2021) | Viewed by 4307

Special Issue 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 intellectually attractive and exciting subjects in a modern science. Due to the physico-chemical properties of studied substances there are several methods and techniques 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 serum-protein ligand interactions by using useful multi-disciplinary techniques applied in laboratories world-wide for investigating the basic principles and practical application especially in the field of pharmaceutical and biomedical applications.     

Dr. Małgorzata Maciążek-Jurczyk
Guest Editor

Manuscript Submission Information

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Keywords

  • serum protein-ligand interactions
  • binding affinity
  • serum protein structure and function

Published Papers (2 papers)

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Research

21 pages, 4254 KiB  
Article
Spectroscopic Studies of Quinobenzothiazine Derivative in Terms of the In Vitro Interaction with Selected Human Plasma Proteins. Part 1
by Aleksandra Owczarzy, Andrzej Zięba, Jadwiga Pożycka, Karolina Kulig, Wojciech Rogóż, Agnieszka Szkudlarek and Małgorzata Maciążek-Jurczyk
Molecules 2021, 26(16), 4776; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26164776 - 06 Aug 2021
Cited by 12 | Viewed by 1836
Abstract
Plasma proteins play a fundamental role in living organisms. They participate in the transport of endogenous and exogenous substances, especially drugs. 5-alkyl-12(H)-quino[3,4-b][1,4]benzothiazinium salts, have been synthesized as potential anticancer substances used for cancer treatment. Most anticancer substances generate a toxic effect on the [...] Read more.
Plasma proteins play a fundamental role in living organisms. They participate in the transport of endogenous and exogenous substances, especially drugs. 5-alkyl-12(H)-quino[3,4-b][1,4]benzothiazinium salts, have been synthesized as potential anticancer substances used for cancer treatment. Most anticancer substances generate a toxic effect on the human body. In order to check the toxicity and therapeutic dosage of these chemicals, the study of ligand binding to plasma proteins is very relevant. The present work presents the first comparative analysis of the binding of one of the 5-alkyl-12(H)-quino[3,4-b][1,4]benzothiazinium derivatives (Salt1) with human serum albumin (HSA), α-1-acid glycoprotein (AGP) and human gamma globulin (HGG), assessed using fluorescence, UV-Vis and CD spectroscopy. In order to mimic in vivo ligand–protein binding, control normal serum (CNS) was used. Based on the obtained data, the Salt1 binding sites in the tertiary structure of all plasma proteins and control normal serum were identified. Both the association constants (Ka) and the number of binding site classes (n) were calculated using the Klotz method. The strongest complex formed was Salt1–AGPcomplex (Ka = 7.35·104 and 7.86·104 mol·L−1 at excitation wavelengths λex of 275 and 295 nm, respectively). Lower values were obtained for Salt1–HSAcomplex (Ka = 2.45·104 and 2.71·104 mol·L−1) and Salt1–HGGcomplex (Ka = 1.41·104 and 1.33·104 mol·L−1) at excitation wavelengths λex of 275 and 295 nm, respectively, which is a positive phenomenon and contributes to the prolonged action of the drug. Salt1 probably binds to the HSA molecule in Sudlow sites I and II; for the remaining plasma proteins studied, only one binding site was observed. Moreover, using circular dichroism (CD), fluorescence and UV-Vis spectroscopy, no effect on the secondary and tertiary structures of proteins in the absence or presence of Salt1 has been demonstrated. Despite the fact that the conducted studies are basic, from the scientific point of view they are novel and encourage further in vitro and in vivo investigations. As a next part of the study (Part 2), the second new synthetized quinobenzothiazine derivative (Salt2) will be analyzed and published. Full article
(This article belongs to the Special Issue Serum Protein-Ligand Interactions)
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12 pages, 2623 KiB  
Article
How Does Glycation Affect Binding Parameters of the Albumin-Gliclazide System in the Presence of Drugs Commonly Used in Diabetes? In Vitro Spectroscopic Study
by Katarzyna Wiglusz, Ewa Żurawska-Płaksej, Anna Rorbach-Dolata and Agnieszka Piwowar
Molecules 2021, 26(13), 3869; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26133869 - 24 Jun 2021
Cited by 4 | Viewed by 1950
Abstract
In this research, the selected drugs commonly used in diabetes and its comorbidities (gliclazide, cilazapril, atorvastatin, and acetylsalicylic acid) were studied for their interactions with bovine serum albumin—native and glycated. Two different spectroscopic methods, fluorescence quenching and circular dichroism, were utilized to elucidate [...] Read more.
In this research, the selected drugs commonly used in diabetes and its comorbidities (gliclazide, cilazapril, atorvastatin, and acetylsalicylic acid) were studied for their interactions with bovine serum albumin—native and glycated. Two different spectroscopic methods, fluorescence quenching and circular dichroism, were utilized to elucidate the binding interactions of the investigational drugs. The glycation process was induced in BSA by glucose and was confirmed by the presence of advanced glycosylation end products (AGEs). The interaction between albumin and gliclazide, with the presence of another drug, was confirmed by calculation of association constants (0.11–1.07 × 104 M−1). The nature of changes in the secondary structure of a protein depends on the drug used and the degree of glycation. Therefore, these interactions may have an influence on pharmacokinetic parameters. Full article
(This article belongs to the Special Issue Serum Protein-Ligand Interactions)
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