DOES hemopressin bind metal ions in vivo?

2016 ◽  
Vol 45 (45) ◽  
pp. 18267-18280 ◽  
Author(s):  
Maurizio Remelli ◽  
Carlo Ceciliato ◽  
Remo Guerrini ◽  
Paulina Kolkowska ◽  
Karolina Krzywoszynska ◽  
...  
Keyword(s):  
Biological Activity ◽  
Metal Ions ◽  
Metal Binding ◽  
Binding Ability ◽  
Metal Binding Ability

The metal-binding ability of hemopressin and its derivatives suggests a possible role of the endogenous metal ions in the biological activity of these neuropeptides.

scholarly journals Recent Advances in Antabuse (Disulfiram): The Importance of its Metal-binding Ability to its Anticancer Activity

2018 ◽  
Vol 25 (4) ◽  
pp. 506-524 ◽  
Author(s):  
Maricela Viola-Rhenals ◽  
Kush R. Patel ◽  
Laura Jaimes-Santamaria ◽  
Guojun Wu ◽  
Jinbao Liu ◽  
...  
Keyword(s):  
Anticancer Activity ◽  
Anticancer Drugs ◽  
Metal Binding ◽  
Biological Activities ◽  
Bibliographic Databases ◽  
Binding Ability ◽  
Biological Aspects ◽  
Metal Binding Ability

Background: Considerable evidence demonstrates the importance of dithiocarbamates especially disulfiram as anticancer drugs. However there are no systematic reviews outlining how their metal-binding ability is related to their anticancer activity. This review aims to summarize chemical features and metal-binding activity of disulfiram and its metabolite DEDTC, and discuss different mechanisms of action of disulfiram and their contributions to the drug's anticancer activity. Methods: We undertook a disulfiram-related search on bibliographic databases of peerreviewed research literature, including many historic papers and in vitro, in vivo, preclinical and clinical studies. The selected papers were carefully reviewed and summarized. Results: More than five hundreds of papers were obtained in the initial search and one hundred eighteen (118) papers were included in the review, most of which deal with chemical and biological aspects of Disulfiram and the relationship of its chemical and biological properties. Eighty one (81) papers outline biological aspects of dithiocarbamates, and fifty seven (57) papers report biological activity of Disulfiram as an inhibitor of proteasomes or inhibitor of aldehyde dehydrogenase enzymes, interaction with other anticancer drugs, or mechanism of action related to reactive oxygen species. Other papers reviewed focus on chemical aspects of dithiocarbamates. Conclusion: This review confirms the importance of chemical features of compounds such as Disulfiram to their biological activities, and supports repurposing DSF as a potential anticancer agent.

scholarly journals Deferoxamine B: A Natural, Excellent and Versatile Metal Chelator

Molecules ◽  
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.

scholarly journals Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveals a role for the disordered C-terminal arm in metal trafficking

2012 ◽  
Vol 441 (3) ◽  
pp. 1017-1035 ◽  
Author(s):  
Katarzyna Banaszak ◽  
Vlad Martin-Diaconescu ◽  
Matteo Bellucci ◽  
Barbara Zambelli ◽  
Wojciech Rypniewski ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Metal Ions ◽  
Metal Binding ◽  
Metal Ion ◽  
Mutual Influence ◽  
Accurate Information ◽  
Metal Ion Binding ◽  
X Ray ◽  
X Ray Absorption

The survival and growth of the pathogen Helicobacter pylori in the gastric acidic environment is ensured by the activity of urease, an enzyme containing two essential Ni2+ ions in the active site. The metallo-chaperone UreE facilitates in vivo Ni2+ insertion into the apoenzyme. Crystals of apo-HpUreE (H. pylori UreE) and its Ni2+- and Zn2+-bound forms were obtained from protein solutions in the absence and presence of the metal ions. The crystal structures of the homodimeric protein, determined at 2.00 Å (apo), 1.59 Å (Ni2+) and 2.52 Å (Zn2+) resolution, show the conserved proximal and solvent-exposed His102 residues from two adjacent monomers invariably involved in metal binding. The C-terminal regions of the apoprotein are disordered in the crystal, but acquire significant ordering in the presence of the metal ions due to the binding of His152. The analysis of X-ray absorption spectral data obtained using solutions of Ni2+- and Zn2+-bound HpUreE provided accurate information of the metal-ion environment in the absence of solid-state effects. These results reveal the role of the histidine residues at the protein C-terminus in metal-ion binding, and the mutual influence of protein framework and metal-ion stereo-electronic properties in establishing co-ordination number and geometry leading to metal selectivity.

scholarly journals An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica

1975 ◽  
Vol 151 (2) ◽  
pp. 459-462 ◽  
Author(s):  
J Colby ◽  
H Dalton ◽  
R Whittenbury
Keyword(s):  
Metal Ions ◽  
Methane Oxidation ◽  
Metal Binding ◽  
Methylomonas Methanica

Extracts of Methylomonas methanica catalyse the O2-and NAD(P)H-dependent disappearance of bromomethane. The activity is unstable at 2 degrees C but is stable at --70 degrees C for several weeks. Bromomethane mono-oxygenase is particulate and is inhibited by metal-binding reagents, by compounds SKF 525A and Lilly 53325, by some metal ions and by acetylene. Evidence is presented that indicates that bromomethane mono-oxygenase is the enzyme responsible for methane oxidation in vivo.

scholarly journals Multinuclear metal-binding ability of a carotene

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Shinnosuke Horiuchi ◽  
Yuki Tachibana ◽  
Mitsuki Yamashita ◽  
Koji Yamamoto ◽  
Kohei Masai ◽  
...  
Keyword(s):  
Metal Binding ◽  
Binding Ability ◽  
Metal Binding Ability

Metal binding ability of microbial natural metal chelators and potential applications

2020 ◽  
Vol 37 (9) ◽  
pp. 1262-1283 ◽  
Author(s):  
Marika Hofmann ◽  
Gerardo Retamal-Morales ◽  
Dirk Tischler
Keyword(s):  
Metal Binding ◽  
Metal Chelators ◽  
Binding Ability ◽  
Potential Applications ◽  
Metal Binding Ability

Metallophores can chelate many different metal and metalloid ions next to iron, make them valuable for many applications.

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