The interaction of actinide and lanthanide ions with hemoglobin and its relevance to human and environmental toxicology

Kumar, Amit; Ali, Manjoor; Ningthoujam, R. S.; Gaikwad, Pallavi S.; Kumar, Mukesh; Nath, Bimalendu B.; Pandey, Badri N.

doi:10.1016/j.jhazmat.2015.12.029

Cited by 64 publications

(30 citation statements)

References 36 publications

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“…In addition to the heme prosthetic group, other metal ions may also bind to the protein if there are potential metal-binding sites. For example, in vitro studies showed that a series of actinide and lanthanide ions such as La 3+ , Ce 3+/4+ , Th 4+ and UO 2 2+ ions may bind to Hb [40]. While Ce 4+ interacts only with the heme moiety, other ions mainly interact with the peptide ligands, causing a decrease in α-helix content.…”

Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

“…While Ce 4+ interacts only with the heme moiety, other ions mainly interact with the peptide ligands, causing a decrease in α-helix content. Moreover, both Th 4+ and UO 2 2+ ions reduce the oxy-form of Hb at a high concentration of >100 µM [40]. Cyt b 5 is a small membrane binding heme protein, and its heme-binding domain is highly negatively charged by a series of acidic residues, forming an "acidic" cluster [41][42][43].…”

Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

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Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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The widespread use of uranium for civilian purposes causes a worldwide concern of its threat to human health due to the long-lived radioactivity of uranium and the high toxicity of uranyl ion (UO 2 2+ ). Although uranyl-protein/DNA interactions have been known for decades, fewer advances are made in understanding their structural-functional impacts. Instead of focusing only on the structural information, this article aims to review the recent advances in understanding the binding of uranyl to proteins in either potential, native, or artificial metal-binding sites, and the structural-functional impacts of uranyl-protein interactions, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Photo-induced protein/DNA cleavages, as well as other impacts, are also highlighted. These advances shed light on the structure-function relationship of proteins, especially for metalloproteins, as impacted by uranyl-protein interactions. It is desired to seek approaches for biological remediation of uranyl ions, and ultimately make a full use of the double-edged sword of uranium.Proteins, especially for metalloproteins, play vital roles in supporting life, including electron-transfer, O 2 -binding and delivery, and catalysis, etc [11][12][13][14][15][16][17][18]. To date, a plenitude of proteins have been shown to interact with UO 2 2+ , such as proteins in blood (human serum albumin, HSA; transferrin, Tf;hemoglobin, Hb), proteins involved in bone growth (osteopontin, OPN; fetuin-A), and the intracellar proteins (metallothionein, MT; cytochromes b 5 /c; Cyt b 5 /c; calmodulin, CaM), etc [19]. Although the structural features of some uranyl-protein complexes are well-documented [7-9], fewer advances are made in understanding the functional impacts of uranyl-protein interactions, with much less for other actinides-proteins interactions, as reviewed by Creff et al. very recently [20]. Instead of focusing only on the structural information, this review highlights the recent advances in understanding the binding of uranyl to proteins, as illustrated in Scheme 1, in either potential, native or artificial metal-binding sites, or the corresponding structural-functional impacts, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Future directions for studying uranyl-protein interactions are also prospected.

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Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

Section: Binding To Potential Metal-binding Sitesmentioning

confidence: 99%

Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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“…CD spectrum of HSA exhibits 2 negative bands at 208 and 222 nm which reflect the characteristic of α‐helix in the advanced structure of protein as these 2 negative peaks are both contributed to n → π * transfer for the peptide bond of α‐helical . CD results can be expressed in mean residue ellipticity (MRE) in deg cm 2 day mol −1 according to the following equation:

italicMRE = \frac{italicObserved CD ((), m deg)}{C_{p} italicnl \times 10}

where C p denotes the molar concentration of the protein, n is the number of amino acid residues, and l is the path length (0.1 cm). The α‐helical contents of free and combined HSA were calculated from MRE values at 208 nm using the equation:

a - italichelix (() %) = \frac{- {MRE}_{208} - 4000}{33000 - 4000}

where MRE 208 is the observed MRE value at 208 nm, 4000 is the MRE of the β form and random coil conformation cross at 208 nm, and 33,000 is the MRE value of a pure α‐helix at 208 nm.…”

Section: Resultsmentioning

confidence: 99%

Study on the molecular recognition action of lamivudine by human serum albumin

Zhang

Zhou

Xia

2018

J of Molecular Recognition

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In this work, the interaction of an anti-HIV drug lamivudine and human serum albumin (HSA) was studied by multispectroscopic and molecular modeling methods. The fluorescence emission spectra showed that the fluorescence of HSA was quenched by lamivudine through static mechanism with HSA-lamivudine complex produced at ground state. According to the binding equilibriums observed at 4 different temperatures, the number of binding site, binding constant, enthalpy change, entropy change, and Gibbs free energy change of the interaction were calculated. The results indicated that there was only 1 main binding site under present concentration condition, and then, the location of this binding site was ascertained by molecular probe experiments using warfarin and ibuprofen as site markers. The interaction was a spontaneous and exothermic process. Hydrogen bonds and van der Waals force were the major power that fixed lamivudine on Sudlow's site I in subdomain IIA of HSA molecule. The distance between donor and acceptor was determined by Förster's nonradiative fluorescence resonance energy transfer theory. Circular dichroism spectra exhibited the alteration of HSA's secondary structures. Molecular modeling investigation revealed the structure of HSA-lamivudine complex, including the conformation of lamivudine in binding site, the amino residues close to lamivudine, and the interaction forces between receptor and ligand. The study may be beneficial to therapists in understanding the distribution of lamivudine in vivo and explaining its drug-resistant mechanism in clinical diagnosis.

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“…The lanthanide series of elements are categorized as hard acids and they form ionic or electrostatic bonds with other elements largely. Various studies related to the interaction of Ce 2+ with biological proteins have been carried out 25,26 . The other lanthanide Gd 2+ is toxic in biological systems as it competes with Ca 2+ ions for all the processes that need Ca 2+ for proper functioning, probably due to the fact that both ions have similar degree of hardness.…”

Section: +mentioning

confidence: 99%

Binding Behavior of Few Lanthanides and Heavy Metal ions with Proteins by Fast and Reliable Affinity Capillary Electrophoresis Method

Alhazm¹,

Albratty²

2017

Orient. J. Chem

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The interaction of two lanthanides Cerium (Ce 3+ ) and Gadolinium (Gd 3+ ) and two heavy metal ions Manganese (Mn 2+ ) and Zinc (Zn 2+ ) with various biological proteins Bovine Serum Albumin, Human Serum Albumin, β-lactoglobulin, Myoglobin and Ovalbumin were studied by using mobility shift affinity capillary electrophoresis. The used ACE method offers fast operation using shorter capillary, small injection volume, adequate short rinsing protocol and lower concentration of samples. The normalized difference of mobility ratio (ΔR/R f ) was used to investigate the possible interaction. All interactions were summarized as ΔR/R f chart and compared. For heavy metal ions, the interactions of Mn 2+ with all proteins were significant with negative ΔR/R f values except with Myoglobin (MB) as its ΔR/Rf close to zero (0.002± 0.03) and one of its cnf(ΔR/R f ) values intersect the zero line indicates insignificant interaction. Very weak interactions between Zn 2+ and all proteins were detected with small +ΔR/Rf values and confidence intervals intersected the zero line. For lanthanides, Cerium (Ce 3+ ) showed weak interactions with BSA, HSA. Whereas, strong interactions were observed with MB and BLACT. Gd 3+ showed almost insignificant interactions with most of the tested proteins except MB, it showed strong interaction with MB in a manner similar to Ce 3+ . Influence of the coordination number of the metal ions and multiple binding sites within the proteins on the signs of ΔR/R f values were discussed in details. Furthermore, the change in protein peak shape was found to be as evident for a possible conformational change for the proteins and their affinity to the metal ions.

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The interaction of actinide and lanthanide ions with hemoglobin and its relevance to human and environmental toxicology

Cited by 64 publications

References 36 publications

Uranyl Binding to Proteins and Structural-Functional Impacts

Uranyl Binding to Proteins and Structural-Functional Impacts

Study on the molecular recognition action of lamivudine by human serum albumin

Binding Behavior of Few Lanthanides and Heavy Metal ions with Proteins by Fast and Reliable Affinity Capillary Electrophoresis Method

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