Correction: Impact of metal binding on the antitumor activity and cellular imaging of a metal chelator cationic imidazopyridine derivative

Mithun Roy; Balabhadrapatruni V. S. K. Chakravarthi; Chelliah Jayabaskaran; Anjali A. Karande; Akhil R. Chakravarty

doi:10.1039/c9dt90223f

Correction: Impact of metal binding on the antitumor activity and cellular imaging of a metal chelator cationic imidazopyridine derivative

Dalton Transactions ◽

10.1039/c9dt90223f ◽

2019 ◽

Vol 48 (42) ◽

pp. 16126-16126

Author(s):

Mithun Roy ◽

Balabhadrapatruni V. S. K. Chakravarthi ◽

Chelliah Jayabaskaran ◽

Anjali A. Karande ◽

Akhil R. Chakravarty

Keyword(s):

Antitumor Activity ◽

Metal Binding ◽

Cellular Imaging ◽

Dalton Trans ◽

Metal Chelator

Correction for ‘Impact of metal binding on the antitumor activity and cellular imaging of a metal chelator cationic imidazopyridine derivative’ by Mithun Roy et al., Dalton Trans., 2011, 40, 4855–4864.

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Impact of metal binding on the antitumor activity and cellular imaging of a metal chelator cationic imidazopyridine derivative

Dalton Transactions ◽

10.1039/c0dt01717e ◽

2011 ◽

Vol 40 (18) ◽

pp. 4855-4864 ◽

Cited By ~ 26

Author(s):

Mithun Roy ◽

Balabhadrapatruni V. S. K. Chakravarthi ◽

Chelliah Jayabaskaran ◽

Anjali A. Karande ◽

Akhil R. Chakravarty

Keyword(s):

Antitumor Activity ◽

Cancer Cells ◽

Metal Binding ◽

Binding Sites ◽

Cellular Imaging ◽

Water Soluble ◽

Photodynamic Effect ◽

Metal Binding Sites ◽

Metal Chelator ◽

Apoptosis In Cancer Cells

Water soluble cationic imidazopyridine species (1) having metal binding sites induces metal-assisted caspase dependent apoptosis in cancer cells and enhanced photodynamic effect in the presence of Fe2+or Zn2+ions.

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Deferoxamine B: A Natural, Excellent and Versatile Metal Chelator

Molecules ◽

10.3390/molecules26113255 ◽

2021 ◽

Vol 26 (11) ◽

pp. 3255

Author(s):

Denise Bellotti ◽

Maurizio Remelli

Keyword(s):

Metal Ions ◽

Metal Binding ◽

Chelation Therapy ◽

Iron Chelation ◽

Binding Ability ◽

Complex Formation Equilibria ◽

Metal Chelator ◽

The Past ◽

Formation Equilibria ◽

Terminal Amino

Deferoxamine B is an outstanding molecule which has been widely studied in the past decade for its ability to bind iron and many other metal ions. The versatility of this metal chelator makes it suitable for a number of medicinal and analytical applications, from the well-known iron chelation therapy to the most recent use in sensor devices. The three bidentate hydroxamic functional groups of deferoxamine B are the centerpiece of its metal binding ability, which allows the formation of stable complexes with many transition, lanthanoid and actinoid metal ions. In addition to the ferric ion, in fact, more than 20 different metal complexes of deferoxamine b have been characterized in terms of their chemical speciation in solution. In addition, the availability of a terminal amino group, most often not involved in complexation, opens the way to deferoxamine B modification and functionalization. This review aims to collect and summarize the available data concerning the complex-formation equilibria in solutions of deferoxamine B with different metal ions. A general overview of the progress of its applications over the past decade is also discussed, including the treatment of iron overload-associated diseases, its clinical use against cancer and neurodegenerative disorders and its role as a diagnostic tool.

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Correction: Photorelease of a metal-binding pharmacophore from a Ru(ii) polypyridine complex

Dalton Transactions ◽

10.1039/d1dt90028e ◽

2021 ◽

Author(s):

Johannes Karges ◽

Ryjul W. Stokes ◽

Seth M. Cohen

Keyword(s):

Metal Binding ◽

Dalton Trans

Correction for ‘Photorelease of a metal-binding pharmacophore from a Ru(ii) polypyridine complex’ by Johannes Karges et al., Dalton Trans., 2021, DOI: 10.1039/D0DT04290K.

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Comparison of localization of metallothionein in tissues of metallothionein-deficient mice

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100141585 ◽

1995 ◽

Vol 53 ◽

pp. 1042-1043

Author(s):

H. Nishimura ◽

R Nishimura ◽

D.L. Adelson ◽

A.E. Michaelska ◽

K.H.A. Choo ◽

...

Keyword(s):

Metal Binding ◽

Immunohistochemical Staining ◽

Squamous Epithelium ◽

Rabbit Antiserum ◽

Slight Modification ◽

Positive Control ◽

Heavy Metal Binding ◽

Critical Organ ◽

Metal Binding Protein ◽

Deficient Mice

Metallothionein (MT), a cysteine-rich heavy metal binding protein, has several isoforms designated from I to IV. Its major isoforms, I and II, can be induced by heavy metals like cadmium (Cd) and, are present in various organs of man and animals. Rodent testes are a critical organ to Cd and it is still a controversial matter whether MT exists in the testis although it is clear that MT is not induced by Cd in this tissue. MT-IV mRNA was found to localize within tongue squamous epithelium. Whether MT-III is present mainly glial cells or neurons has become a debatable topic. In the present study, we have utilized MT-I and II gene targeted mice and compared MT localization in various tissues from both MT-deficient mice and C57Black/6J mice (C57BL) which were used as an MT-positive control. For MT immunostaining, we have used rabbit antiserum against rat MT-I known to cross-react with mammalian MT-I and II and human MT-III. Immunohistochemical staining was conducted by the method described in the previous paper with a slight modification after the tissues were fixed in HistoChoice and embedded in paraffin.

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A new family of fluorescent calcium indicators designed to resist leakage or for measuring calcium near membranes

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100168578 ◽

1994 ◽

Vol 52 ◽

pp. 168-169

Author(s):

Martin Poenie ◽

Akwasi Minta ◽

Charles Vorndran

Keyword(s):

Metal Binding ◽

Acetoxymethyl Ester ◽

Binding Properties ◽

Fura 2 ◽

New Family ◽

Anion Transporter ◽

Calcium Indicator ◽

Calcium Indicators ◽

High Calcium ◽

Intracellular Compartmentalization

The use of fura-2 as an intracellular calcium indicator is complicated by problems of rapid dye leakage and intracellular compartmentalization which is due to a probenecid sensitive anion transporter. In addition there is increasing evidence for localized microdomains of high calcium signals which may not be faithfully reported by fura-2.We have developed a new family of fura-2 analogs aimed at addressing some of these problems. These new indicators are based on a modified bapta which can be readily derivatized to produce fura-2 analogs with a variety of new properties. The modifications do not affect the chromophore and have little impact on the spectral and metal binding properties of the indicator. One of these new derivatives known as FPE3 is a zwitterionic analog of fura-2 that can be loaded into cells as an acetoxymethyl ester and whose retention in cells is much improved. The improved retention of FPE3 is important for both cuvettebased measurements of cell suspensions and for calcium imaging.

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Structures of c-di-GMP/cGAMP degrading phosphodiesterase VcEAL: identification of a novel conformational switch and its implication

Biochemical Journal ◽

10.1042/bcj20190399 ◽

2019 ◽

Vol 476 (21) ◽

pp. 3333-3353 ◽

Cited By ~ 3

Author(s):

Malti Yadav ◽

Kamalendu Pal ◽

Udayaditya Sen

Keyword(s):

Active Site ◽

Metal Binding ◽

Metal Ion ◽

Triosephosphate Isomerase ◽

Catalytic Mechanism ◽

Degradation Mechanism ◽

Structural Basis ◽

Conserved Residues ◽

Phosphodiester Bond ◽

Cyclic Dinucleotides

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.

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