Alteration of human serum albumin binding properties induced by modifications: A review

Maciążek-Jurczyk, Małgorzata; Szkudlarek, Agnieszka; Chudzik, Mariola; Pożycka, Jadwiga; Sułkowska, Anna

doi:10.1016/j.saa.2017.05.023

Cited by 64 publications

(54 citation statements)

References 124 publications

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“…HSA was employed in this study as a model protein to understand protein–ligand complex interaction. HSA is the most abundant protein in the serum plasma with a molecular weight of 66.5 kDa . This protein is synthesized in the liver and its principal function is to stabilize the osmotic pressure for the proper distribution of fluids in the body.…”

Section: Resultsmentioning

confidence: 99%

Synthesis and structural studies of 16‐ferrocenemethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol and its interaction with human serum albumin by fluorescence spectroscopy and in silico docking approaches

Carmona‐Negrón

Liboy-Lugo

Santana

et al. 2020

Applied Organom Chemis

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16‐Ferrocenylmethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol crystallizes in a triclinic unit cell and P1 space group. It contains four crystallographic independent molecules in the unit, representing four different conformers of the ferrocene–hormone conjugate. It provides evidence of a low rotational barrier around C19–C20 and the existence of alpha and beta conformers. The four conformers are interconnected by hydrogen bonds through hydroxyl groups of rings A and D. Density functional theory studies show the rotational barrier energy to be 4.96 Kcal/mol and the preferred conformer has a dihedral angle φ2 (defined as C16–C19–C20–C21) of 85.79°. This angle represents the conformer with the lowest steric strains. Docking studies between the subject compound and human serum albumin (HSA) showed that the most likely binding pocket of HSA is drug‐binding site 2. Quenching fluorescence spectroscopy was used to study HSA–ferrocene conjugate interaction and results showed that the complex formation was static and dominated by van der Waals and electrostatic/hydrogen bonding interactions.

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Section: Resultsmentioning

confidence: 99%

Synthesis and structural studies of 16‐ferrocenemethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol and its interaction with human serum albumin by fluorescence spectroscopy and in silico docking approaches

Carmona‐Negrón

Liboy-Lugo

Santana

et al. 2020

Applied Organom Chemis

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“…It was found that with age the rigidity of the scleral matrix increases, the degree of fiber straightening and the mechanical anisotropy in the peripapillary sclera decreases [69]. The aging of organism is accompanied by structural and functional modifications of macromolecules [70]. The changes that occur in the tissues of the organism under the development of diabetes mellitus are investigated both in laboratory animals using experimental models [9][10][11]17, 39, 40, 42, 45-47, [71][72][73][74][75][76][77] and directly in patients in the course of clinical examination [12,35,[78][79][80][81][82][83][84][85][86][87].…”

Section: Classification Of Diabetes Mellitusmentioning

confidence: 99%

“…The glycation is a result of the interaction between the glucose molecules and the proteins, which leads to the change of protein structure and to the restriction of To study the glycation of proteins, both the samples of tissues and cells from the objects with natural or artificially induced diabetes mellitus (in vivo glycation), as well as the samples that has been glycated under in vitro conditions are used. Studies of in vitro glycation refer, for example, to human placental type IV collagen, performed by fluorescence analysis, as well as by electrophoresis and densitometry [134]; collagen of bovine skin -using multiphoton microscopy [34]; hemoglobin -by optical coherent tomography [135][136][137], refractometry and IR spectroscopy [122], as well as biochemical analysis [138]; albumin -using fluorescence spectroscopy [70], refractometry [122], and terahertz spectroscopy [138]; collagen of the tendon -through biochemical and biomechanical analyzes [139], as well as to collagen hydrogels -using multispectral fluorescence life time imaging (FLIM) [140]; by incubation in ribose [37,134,139,140], glucose [70,122,135,138,141] or fructose [70,141] solutions. All of them show a sufficiently effective glycation of proteins during 10-11 days of incubation, a change in the mechanical properties of tissues due to the formation of collagen cross-links.…”

Section: Glycation and Non-enzymatic Glycation Of Proteinsmentioning

confidence: 99%

“…These serious complications are due to the glycation of proteins in vascular walls permanently washed by blood in the presence of increased free glucose content in blood [41,129,135,138]. Different methods are used to determine glycated hemoglobin or albumin, such as ion exchange, affine, or liquid chromatography, electrophoresis, colorimetric and immunochemical methods [70,143]. First, these methods are invasive, since they imply blood sampling from the patient's vein.…”

Section: Blood and Cardiovascular Systemmentioning

confidence: 99%

“…Since the high level of blood glucose leads to the growth of its content in the interstitial fluid, the glycation affects not only the blood proteins, such as albumin and hemoglobin [70,129,135,138,155], but also other proteins of the organism tissues. For example, in Refs.…”

Section: Different Tissuesmentioning

confidence: 99%

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Optical and structural properties of biological tissues under diabetes mellitus

Tuchina

Tuchin

2018

J-BPE

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Abstract. Diabetes mellitus is a serious social and economic problem of modern society because it is widespread and fraught with numerous complications. Therefore, it is necessary to search for new methods of diabetes mellitus diagnostics and treatment and to improve the existing ones, which, in turn, requires thorough investigation of the disease development mechanisms, as well as elaboration of simple and reliable methods and criteria for detecting the complication precursors. In connection with the solution of these problems, in the paper we present an analytical review of recent publications devoted to the study of the changes of structural and optical properties of biological tissues under the conditions of diabetes mellitus development using in vitro models of glycated tissues, in vivo experimental models of diabetes in laboratory animals, and clinical studies.

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Studies of the Novel Bioactive Acridine‐1,3‐thiazolidin‐4‐one Derivatives With Human Serum Albumin Using Fluorescence Spectroscopy and Molecular Modelling

Konkoľová,

Miháliková,

Nowak

et al. 2024

Luminescence

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In this study, we employ spectroscopic, thermodynamic and molecular docking approaches to identify the mechanism by which thiazolidinone derivatives 4a–4d bind with human serum albumin. It has been suggested that the affinity of the interaction of derivatives 4a–4d with HSA is within the optimal range necessary for the transportation and distribution of compounds within the organism. The binding constant values for the derivative/HSA complexes were found to be 0.03–5.87 × 105 M−1. Both ΔH0 and ΔS0 values were negative, which indicates that binding occurs mainly through van der Waals forces and hydrogen bonding. The negative values calculated for ΔG0 indicate that the binding of derivatives 4a–4d with HSA is a spontaneous process. Our study also reveals that derivatives 4a–4d bind to the subdomain IB (Site III) of HSA and that this binding alters the conformation and thermodynamic stability of HSA. Molecular docking simulations suggest that the main binding forces are van der Waals interactions, hydrophobic interactions and hydrogen bonds. The studied compounds showed weak DPPH‐scavenging activity at all of the tested concentrations. The results suggest that compound 4b with a phenyl substituent at the nitrogen atom of the 1,3‐thiazolidin‐4‐one moiety can be considered the most potent antioxidant in the series.

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Alteration of human serum albumin binding properties induced by modifications: A review

Cited by 64 publications

References 124 publications

Synthesis and structural studies of 16‐ferrocenemethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol and its interaction with human serum albumin by fluorescence spectroscopy and in silico docking approaches

Synthesis and structural studies of 16‐ferrocenemethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol and its interaction with human serum albumin by fluorescence spectroscopy and in silico docking approaches

Optical and structural properties of biological tissues under diabetes mellitus

Studies of the Novel Bioactive Acridine‐1,3‐thiazolidin‐4‐one Derivatives With Human Serum Albumin Using Fluorescence Spectroscopy and Molecular Modelling

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