Evaluation of the Binding Ability of a Novel Dioxatetraazamacrocyclic Receptor that Contains Two Phenanthroline Units:  Selective Uptake of Carboxylate Anions

2007 ◽  
Vol 72 (11) ◽  
pp. 4023-4034 ◽  
Author(s):  
Carla Cruz ◽  
Rita Delgado ◽  
Michael G. B. Drew ◽  
Vítor Félix
Keyword(s):  
Binding Ability ◽  
Selective Uptake ◽  
Carboxylate Anions

Evaluation of the binding ability of tetraaza[2]arene[2]triazine receptors anchoring l-alanine units for aromatic carboxylate anions

Tetrahedron ◽  
2012 ◽  
Vol 68 (2) ◽  
pp. 670-680 ◽  
Author(s):  
Ana I. Vicente ◽  
João M. Caio ◽  
João Sardinha ◽  
Cristina Moiteiro ◽  
Rita Delgado ◽  
...  
Keyword(s):  
Binding Ability ◽  
Carboxylate Anions ◽  
Aromatic Carboxylate

Treponema, Iron and Neurodegeneration

2018 ◽  
Vol 15 (8) ◽  
pp. 716-722 ◽  
Author(s):  
A. Jolivet-Gougeon ◽  
M. Bonnaure-Mallet
Keyword(s):  
Iron Metabolism ◽  
Plasma Proteins ◽  
Iron Homeostasis ◽  
Neurological Diseases ◽  
Host Cells ◽  
Loss Of Function ◽  
Binding Ability ◽  
Iron Binding Proteins ◽  
Oxidative Species ◽  
Iron Reductase

Spirochetes are suspected to be linked to the genesis of neurological diseases, including neurosyphillis or neurodegeneration (ND). Impaired iron homeostasis has been implicated in loss of function in several enzymes requiring iron as a cofactor, formation of toxic oxidative species, inflammation and elevated production of beta-amyloid proteins. This review proposes to discuss the link that may exist between the involvement of Treponema spp. in the genesis or worsening of ND, and iron dyshomeostasis. Proteins secreted by Treponema can act directly on iron metabolism, with hemin binding ability (HbpA and HbpB) and iron reductase able to reduce the central ferric iron of hemin, iron-containing proteins (rubredoxin, neelaredoxin, desulfoferrodoxin metalloproteins, bacterioferritins etc). Treponema can also interact with cellular compounds, especially plasma proteins involved in iron metabolism, contributing to the virulence of the syphilis spirochetes (e.g. treponemal motility and survival). Fibronectin, transferrin and lactoferrin were also shown to be receptors for treponemal adherence to host cells and extracellular matrix. Association between Treponema and iron binding proteins results in iron accumulation and sequestration by Treponema from host macromolecules during systemic and mucosal infections.

scholarly journals Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure.

1994 ◽  
Vol 14 (11) ◽  
pp. 7557-7568 ◽  
Author(s):  
J Zuo ◽  
R Baler ◽  
G Dahl ◽  
R Voellmy
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Dna Binding ◽  
Hydrophobic Interactions ◽  
Coiled Coil ◽  
Heat Shock Transcription Factor ◽  
Single Amino Acid ◽  
Binding Ability ◽  
Heat Shock Element

Heat stress regulation of human heat shock genes is mediated by human heat shock transcription factor hHSF1, which contains three 4-3 hydrophobic repeats (LZ1 to LZ3). In unstressed human cells (37 degrees C), hHSF1 appears to be in an inactive, monomeric state that may be maintained through intramolecular interactions stabilized by transient interaction with hsp70. Heat stress (39 to 42 degrees C) disrupts these interactions, and hHSF1 homotrimerizes and acquires heat shock element DNA-binding ability. hHSF1 expressed in Xenopus oocytes also assumes a monomeric, non-DNA-binding state and is converted to a trimeric, DNA-binding form upon exposure of the oocytes to heat shock (35 to 37 degrees C in this organism). Because endogenous HSF DNA-binding activity is low and anti-hHSF1 antibody does not recognize Xenopus HSF, we employed this system for mapping regions in hHSF1 that are required for the maintenance of the monomeric state. The results of mutagenesis analyses strongly suggest that the inactive hHSF1 monomer is stabilized by hydrophobic interactions involving all three leucine zippers which may form a triple-stranded coiled coil. Trimerization may enable the DNA-binding function of hHSF1 by facilitating cooperative binding of monomeric DNA-binding domains to the heat shock element motif. This view is supported by observations that several different LexA DNA-binding domain-hHSF1 chimeras bind to a LexA-binding site in a heat-regulated fashion, that single amino acid replacements disrupting the integrity of hydrophobic repeats render these chimeras constitutively trimeric and DNA binding, and that LexA itself binds stably to DNA only as a dimer but not as a monomer in our assays.

scholarly journals Disruption of key NADH-binding pocket residues of the Mycobacterium tuberculosis InhA affects DD-CoA binding ability

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Daniel J. Shaw ◽  
Kirsty Robb ◽  
Beatrice V. Vetter ◽  
Madeline Tong ◽  
Virginie Molle ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Binding Pocket ◽  
Binding Ability

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.

In Vitro PAH-Binding Ability of Lactobacillus brevis TD4

2021 ◽  
pp. 1-17
Author(s):  
Mojtaba Yousefi ◽  
Nasim Khorshidian ◽  
Hedayat Hosseini
Keyword(s):  
Lactobacillus Brevis ◽  
Binding Ability
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