Arsenical grafted membranes for immobilization of thioredoxin-like proteins

Carbajal, María Laura; Espinoza, Silvia Lorena Soto; Valdez, Silvina; Poskus, Edgardo; Smolko, Eduardo E.; Grasselli, Mariano

doi:10.1016/j.reactfunctpolym.2009.07.001

Cited by 11 publications

(7 citation statements)

References 24 publications

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“…73,79 A summary of arsenic affinity resins is listed in Table 3. There are several varieties of PAO affinity resins including Sepharose, 73,74,[80][81][82][83][84] Affigel, 78,85 Eupergit C beads, 86 carboxymethyl (CM)-Bio-Gel supports, 87 and Glycidyl methacrylate grafted macroporous polysulfone membranes 20 coupled to one of the following arsenic functional groups: p-aminophenylarsine oxide (PAPAO), 73,74,78,[84][85][86][87][88] p-[(bromoacetyl)-amino]phenylarsenoxide (BrAcNPAsO), 80 Cymelarsan, 81 or p-arsanilic acid (PAPA). 82,83,88 An atom spacer is frequently included between the support and the arsenic moiety.…”

Section: Arsenic Affinity Chromatographymentioning

confidence: 99%

“…There are several varieties of PAO affinity resins including Sepharose, 73,74,[80][81][82][83][84] Affigel, 78,85 Eupergit C beads, 86 carboxymethyl (CM)-Bio-Gel supports, 87 and Glycidyl methacrylate grafted macroporous polysulfone membranes 20 coupled to one of the following arsenic functional groups: p-aminophenylarsine oxide (PAPAO), 73,74,78,[84][85][86][87][88] p-[(bromoacetyl)-amino]phenylarsenoxide (BrAcNPAsO), 80 Cymelarsan, 81 or p-arsanilic acid (PAPA). 82,83,88 An atom spacer is frequently included between the support and the arsenic moiety. The biarsenical fluorescein dye FlAsH can also be incorporated into an affinity resin that binds to proteins containing the sequence CCXXCC in an a-helix.…”

Section: Arsenic Affinity Chromatographymentioning

confidence: 99%

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Therapeutic and analytical applications of arsenic binding to proteins

et al. 2015

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Arsenic binding to proteins plays a pivotal role in the health effects of arsenic. Further knowledge of arsenic binding to proteins will advance the development of bioanalytical techniques and therapeutic drugs. This review summarizes recent work on arsenic-based drugs, imaging of cellular events, capture and purification of arsenic-binding proteins, and biosensing of arsenic. Binding of arsenic to the promyelocytic leukemia fusion oncoprotein (PML-RARα) is a plausible mode of action leading to the successful treatment of acute promyelocytic leukemia (APL). Identification of other oncoproteins critical to other cancers and the development of various arsenicals and targeted delivery systems are promising approaches to the treatment of other types of cancers. Techniques for capture, purification, and identification of arsenic-binding proteins make use of specific binding between trivalent arsenicals and the thiols in proteins. Biarsenical probes, such as FlAsH-EDT2 and ReAsH-EDT2, coupled with tetracysteine tags that are genetically incorporated into the target proteins, are used for site-specific fluorescence labelling and imaging of the target proteins in living cells. These allow protein dynamics and protein-protein interactions to be studied. Arsenic affinity chromatography is useful for purification of thiol-containing proteins, and its combination with mass spectrometry provides a targeted proteomic approach for studying the interactions between arsenicals and proteins in cells. Arsenic biosensors evolved from the knowledge of arsenic resistance and arsenic binding to proteins in bacteria, and have now been developed into analytical techniques that are suitable for the detection of arsenic in the field. Examples in the four areas, arsenic-based drugs, imaging of cellular events, purification of specific proteins, and arsenic biosensors, demonstrate important therapeutic and analytical applications of arsenic protein binding.

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Section: Arsenic Affinity Chromatographymentioning

confidence: 99%

Section: Arsenic Affinity Chromatographymentioning

confidence: 99%

Therapeutic and analytical applications of arsenic binding to proteins

et al. 2015

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“…Trx, as well as many other tumor-related proteins such as thioredoxin reductase and poly(ADP-ribose)polymerase, is known to bind arsenic [7]. In this work, we evaluated APAO-FITC, a previously synthesized fluorescent arsenic compound that was able to induce apoptosis in a leukemia cell model and to label the apoptotic cell population fluorescently [17], as a labeling probe for Trx.…”

Section: Discussionmentioning

confidence: 99%

“…The thioredoxin 1 used in this work is a histidine-patch thioredoxin system that was purified as described previously by Carbajal et al [7] from an Escherichia coli TOP10 strain transformed with the pThioHis plasmid (Invitrogen, Carlsbad, CA, USA). Briefly, this strain was grown in Luria-Bertani medium (1 % tryptone, 0.5 % yeast extract, 1 % NaCl) containing 0.1 mg/ml ampicillin at 37 °C to an optical density of 0.5 at 550 nm.…”

Section: Trx Purificationmentioning

confidence: 99%

An Arsenic Fluorescent Compound as a Novel Probe to Study Arsenic-Binding Proteins

et al. 2012

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Arsenic-binding proteins are under continuous research. Their identification and the elucidation of arsenic/protein interaction mechanisms are important because the biological effects of these complexes may be related not only to arsenic but also to the arsenic/protein structure. Although many proteins bearing a CXXC motif have been found to bind arsenic in vivo, new tools are necessary to identify new arsenic targets and allow research on protein/arsenic complexes. In this work, we analyzed the performance of the fluorescent compound APAO-FITC (synthesized from p-aminophenylarsenoxide, APAO, and fluorescein isothiocyanate, FITC) in arsenic/protein binding assays using thioredoxin 1 (Trx) as an arsenic-binding protein model. The Trx-APAO-FITC complex was studied through different spectroscopic techniques involving UV-Vis, fluorescence, atomic absorption, infrared and circular dichroism. Our results show that APAO-FITC binds efficiently and specifically to the Trx binding site, labeling the protein fluorescently, without altering its structure and activity. In summary, we were able to study a protein/arsenic complex model, using APAO-FITC as a labeling probe. The use of APAO-FITC in the identification of different protein and cell targets, as well as in in vivo biodistribution studies, conformational studies of arsenic-binding proteins, and studies for the design of drug delivery systems for arsenic anti-cancer therapies, is highly promising.

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“…Surface modification can confer reactivity and new physicochemical properties. Currently, some materials are modified in order to use them as new systems for ion exchange chromatographic separation [12,13], adsorptive fibers with high capacity immobilizing pseudo-affinity ligands [14,15] or as a support for immobilization of enzymes and cells [16]. The application of these materials to a real purification process has been demonstrated [13,17].…”

mentioning

confidence: 99%

Porous Materials in the Bioprocessing Area

Sánchez¹

2015

J Bioprocess Biotech

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Arsenical grafted membranes for immobilization of thioredoxin-like proteins

Cited by 11 publications

References 24 publications

Therapeutic and analytical applications of arsenic binding to proteins

Therapeutic and analytical applications of arsenic binding to proteins

An Arsenic Fluorescent Compound as a Novel Probe to Study Arsenic-Binding Proteins

Porous Materials in the Bioprocessing Area

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