Serum Albumins Guided Plasmonic Nanoassemblies with Opposite Chiralities

The interactions of novel anti-cancer therapeutic agents with the different plasma and tissue components, specifically serum albumins, have lately gained considerable attention due to the significant influence of such interactions on the pharmacokinetics and/or -dynamics of this important class of therapeutics. Nazartinib (EGF 816; NAZ) is a new anti-cancer candidate proposed as a third-generation epidermal growth factor receptor tyrosine kinase inhibitor that is being developed and clinically tested for the management of non-small cell lung cancer. The current study aimed to characterize the interaction between NAZ and human serum albumin (HSA) using experimental and theoretical approaches. Experimental results of fluorescence quenching of HSA induced by NAZ revealed the development of a statically formed complex between NAZ and HSA. Interpretation of the observed fluorescence data using Stern–Volmer, Lineweaver–Burk and double-log formulae resulted in binding constants for HSA-NAZ complex in the range of (2.34–2.81) × 10 4 M –1 over the studied temperatures. These computed values were further used to elucidate thermodynamic attributes of the interaction, which showed that NAZ spontaneously binds to HSA with a postulated electrostatic force-driven interaction. This was further verified by theoretical examination of the NAZ docking on the HSA surface that revealed an HSA-NAZ complex where NAZ is bound to HSA Sudlow site I driven by hydrogen bonding in addition to electrostatic forces in the form of pi-H bond. The HSA binding pocket for NAZ was shown to encompass ARG 257, ARG 222, LYS 199 and GLU 292 with a total binding energy of −25.59 kJ mol –1 .

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Streptococcus pneumoniae Surface Adhesin PfbA Exhibits Host Specificity by Binding to Human Serum Albumin but Not Bovine, Rabbit and Porcine Serum Albumins

The Protein Journal ◽

10.1007/s10930-019-09875-y ◽

2019 ◽

Cited By ~ 1

Author(s):

Sreejanani Sankar ◽

Masaya Yamaguchi ◽

Shigetada Kawabata ◽

Karthe Ponnuraj

Keyword(s):

Streptococcus Pneumoniae ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Host Specificity ◽

Serum Albumins ◽

Porcine Serum

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The effect of ligand presaturation on the interaction of serum albumins with an immobilized Cibacron Blue 3G-A studied by affinity gel electrophoresis

Biochemical Journal ◽

10.1042/bj1990465 ◽

1981 ◽

Vol 199 (3) ◽

pp. 465-472 ◽

Cited By ~ 22

Author(s):

E C Metcalf ◽

B Crow ◽

P D G Dean

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Dissociation Constant ◽

Gel Electrophoresis ◽

Dissociation Constants ◽

Serum Albumins ◽

Albumin Ratio ◽

Cibacron Blue ◽

Affinity Gel Electrophoresis

The interaction of the immobilized triazine dye Cibacron Blue 3G-A with rat, rabbit, sheep, goat, bovine and human serum albumins was studied by affinity gel electrophoresis. Dissociation constants were estimated in each instance and showed human serum albumin to have a significantly higher affinity for the dye than did albumin from any other species. Pretreatment of the defatted proteins with bilirubin (3 mol of bilirubin/mol of protein) did not increase the dissociation constants of the serum albumins, whereas pretreatment with palmitate (7 mol of palmitate/mol of protein) increased the dissociation constant in all cases: 3-fold for human serum albumin, 15-fold for other serum albumins. Increasing the bilirubin/albumin ratio (to 7:1) did not affect the dissociation constant of the albumins studied. Decreasing the palmitate/albumin ratio decreased the dissociation constant for human serum albumin, but did not affect those of bovine and rat albumins. Altering the chain length of the presaturating fatty acid dramatically changed the dissociation constant of both human and bovine serum albumins. Butyrate, hexanoate, octanoate and decanoate did not significantly influence the dissociation constants of bovine and human serum albumins for Cibacron Blue, whereas laurate, myristate and palmitate greatly increased the dissociation constant. These data are discussed in relationship to the behaviour of albumins during dye--agarose column chromatography. In Addendum the effect of nucleotide presaturation on the interaction between Bacillus stearothermophilus 6-phosphogluconate dehydrogenase and the immobilized triazine dyes Cibacron Blue 3G-A and Procion Red HE-3B was examined, and the implications for dye--ligand chromatography are discussed.

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Synthesis and Comparative Study of Nanoparticles Derived from Bovine and Human Serum Albumins

Polymers ◽

10.3390/polym12061301 ◽

2020 ◽

Vol 12 (6) ◽

pp. 1301 ◽

Cited By ~ 2

Author(s):

Yerkeblan Tazhbayev ◽

Olzhas Mukashev ◽

Meiram Burkeyev ◽

Vladimir I. Lozinsky

Keyword(s):

Human Serum Albumin ◽

Bovine Serum Albumin ◽

Drug Release ◽

Serum Albumin ◽

Human Serum ◽

Release Profile ◽

Serum Albumins ◽

Drug Release Profile ◽

Protein Nanoparticles ◽

Inclusion Methods

This study describes the preparation of nanoparticles derived from bovine serum albumin (BSA) in comparison with the formation of nanoparticles composed of human serum albumin (HSA), when the same preparation procedure was used in both cases. To obtain protein nanoparticles, the method of desolvation with ethanol was employed, followed by the stabilization with urea and cysteine. It was shown that, upon transition from HSA to BSA, the particles with smaller sizes and with a narrower polydispersity were formed. The possibility of the immobilization of the antitumor drug hydroxyurea in such protein nanoparticles by adsorption and inclusion methods has been shown. The drug release profile from the polymer matrix was established.

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Spectroscopic Technique-Based Comparative Investigation on the Interaction of Theaflavins with Native and Glycated Human Serum Albumin

Molecules ◽

10.3390/molecules24173171 ◽

2019 ◽

Vol 24 (17) ◽

pp. 3171 ◽

Cited By ~ 4

Author(s):

Jinhui Xu ◽

Mengyuan Wang ◽

Yizhe Zheng ◽

Lin Tang

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Three Dimensional ◽

Black Tea ◽

Comparative Investigation ◽

Spectroscopic Technique ◽

Serum Albumins ◽

Hydrophobic Force ◽

Site Competition

Theaflavin is a kind of multi-pharmacological and health beneficial black tea factor. The aim of this study is to investigate the mechanisms by which theaflavin interacts with glycosylated and non-glycosylated serum albumins and compares their binding properties. Fluorescence and ultraviolet spectra indicated that theaflavin interacted with native and glycated human serum albumin through a static quenching mechanism and had a higher degree of quenching of human serum albumin. The thermodynamic parameters revealed that the combinations of theaflavin with native and glycated human serum albumin were a spontaneous endothermic reaction, and the hydrophobic force was a major driving force in the interaction process. Zeta potential, particle size, synchronous fluorescence, three-dimensional fluorescence spectroscopy and circular dichroism further clarified the effect of theaflavin on the conformation of human serum albumin structure were more pronounced. In addition, site competition experiments and molecular docking technique confirmed that the binding sites of theaflavin on both native and glycated human serum albumin were bound at site II. This study had investigated the effects of glycation on the binding of HSA with polyphenols and the potential nutriology significance of these effects.

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Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A

Biochemical Journal ◽

10.1042/bj1890027 ◽

1980 ◽

Vol 189 (1) ◽

pp. 27-34 ◽

Cited By ~ 106

Author(s):

R J Leatherbarrow ◽

P D Dean

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Sites ◽

Serum Albumins ◽

Fatty Acid Binding ◽

Cibacron Blue ◽

Structural Analogues ◽

Bilirubin Binding ◽

Sepharose 4B

The interaction of Cibacron Blue F3G A-Sepharose 4B with several serum albumins was studied. Although all albumins used were fond to bind to this adsorbent, human serum albumin was bound to a far greater extent than were the others. From the results of competition experiments and n.m.r. studies of Cibacron Blue and/or bilirubin binding to human serum albumin it is proposed that the mechanism of the interaction between human serum albumin and cibacron Blue is consistent wit Cibacron Blue binding to bilirubin-binding sites. In contrast with these findings with human serum albumin, there is little or no interaction of Cibacron Blue and the bilirubin-binding sites of albumins from rabbit, horse, bovine or sheep sera, although some interaction occurs between Cibacron Blue and the fatty acid-binding sites of these proteins. Structural analogues of Cibacron Blue have been used to investigate the binding of albumins to these ligands.

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Interaction of the Coffee Diterpenes Cafestol and 16-O-Methyl-Cafestol Palmitates with Serum Albumins

International Journal of Molecular Sciences ◽

10.3390/ijms21051823 ◽

2020 ◽

Vol 21 (5) ◽

pp. 1823

Author(s):

Federico Berti ◽

Luciano Navarini ◽

Elena Guercia ◽

Ana Oreški ◽

Alessandra Gasparini ◽

...

Keyword(s):

Circular Dichroism ◽

Fatty Acid ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Biologically Active ◽

Aliphatic Chain ◽

Serum Albumins ◽

Complex Behaviour ◽

Circular Dichroïsm

The main coffee diterpenes cafestol, kahweol, and 16-O-methylcafestol, present in the bean lipid fraction, are mostly esterified with fatty acids. They are believed to induce dyslipidaemia and hypercholesterolemia when taken with certain types of coffee brews. The study of their binding to serum albumins could help explain their interactions with biologically active xenobiotics. We investigated the interactions occurring between cafestol and 16-O-methylcafestol palmitates with Bovine Serum Albumin (BSA), Human Serum Albumin (HSA), and Fatty Free Human Serum Albumin (ffHSA) by means of circular dichroism and fluorimetry. Circular Dichroism (CD) revealed a slight change (up to 3%) in the secondary structure of fatty-free human albumin in the presence of the diterpene esters, suggesting that the aliphatic chain of the palmitate partly occupies one of the fatty acid sites of the protein. A warfarin displacement experiment was performed to identify the binding site, which is probably close but not coincident with Sudlow site I, as the affinity for warfarin is enhanced. Fluorescence quenching titrations revealed a complex behaviour, with Stern–Volmer constants in the order of 103–104 Lmol−1. A model of the HSA-warfarin-cafestol palmitate complex was obtained by docking, and the most favourable solution was found with the terpene palmitate chain inside the FA4 fatty acid site and the cafestol moiety fronting warfarin at the interface with site I.

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How human serum albumin‐selective DNA aptamer binds to bovine and canine serum albumins

Biopolymers ◽

10.1002/bip.23421 ◽

2021 ◽

Vol 112 (3) ◽

Author(s):

Nattapon Kuntip ◽

Deanpen Japrung ◽

Prapasiri Pongprayoon

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Dna Aptamer ◽

Serum Albumins ◽

Canine Serum

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Microcalorimetric study of the interaction of human and bovine serum albumins with tryptophan and tryptophan analogs

Canadian Journal of Biochemistry ◽

10.1139/o82-013 ◽

1982 ◽

Vol 60 (2) ◽

pp. 91-99 ◽

Cited By ~ 3

Author(s):

Hong Phuong-Nguyen ◽

Hélène Bruderlein ◽

Geneviève Delmas ◽

Yvon Pépin

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Bovine Serum ◽

Unexpected Finding ◽

Serum Albumins ◽

Huggins Constant ◽

Physicochemical Data ◽

Different Sources ◽

Good Agreement

The thermodynamic parameters for the protein–ligand binding have been obtained by microcalorimetry on three albumin samples (fatty acid free human serum albumin (I), fraction V human serum albumin (II), and fraction V bovine serum albumin (III)) bound with L-tryptophan (A) and three-ring tryptophan analogs (B and B*). The percentage, u, of binding molecules (equivalent to the number of sites) is found to be 1.0 for I and 0.65 for II (in good agreement with dialysis results on the same systems) and 1.0 for III.The large negative ΔH(bind) (−27.2 to −33.2 kJ∙mol−1) constitutes the main contribution to ΔG(bind) (−23.0 to −31.2 kJ·mol−1). The better binding of I–III towards B and B* compared with A is due to ΔS(bind) being less negative. This is interpreted as a lesser loss of entropy for the three-ring ligands than for the normal tryptophan when they are bound.Data obtained on the proteins (heat of dilution; Huggins' constant, k′) correlate well with u or Qmax. This indicates that these physicochemical data could be used to characterize and compare rapidly some albumins of different sources. The unexpected finding that the parameters of I and III are nearer to each other than they are from II is discussed.

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