Tunable Biopolymers for Heavy Metal Removal

Košťál, Jan; Mulchandani, Ashok; Chen, Wilfred

doi:10.1021/ma001973m

Cited by 104 publications

(99 citation statements)

References 21 publications

(39 reference statements)

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“…It is possible to isolate glyco-polypeptides using the interaction between the capture molecule and the sugar group [86] (Figure 8). It has also been shown that ELPs fused to an appropriate fusion partner can bind to heavy metals such as mercury [87], arsenic [88] or cadmium [89,90], and facilitate the rapid isolation of these toxic metal contaminants.…”

Section: Applications Of Elp-based Protein Purification-as the Princimentioning

confidence: 99%

Peptide-based biopolymers in biomedicine and biotechnology

Chow

Nunalee

Lim

et al. 2008

Materials Science and Engineering: R: Reports

286

231

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Peptides are emerging as a new class of biomaterials due to their unique chemical, physical, and biological properties. The development of peptide-based biomaterials is driven by the convergence of protein engineering and macromolecular self-assembly. This review covers the basic principles, applications, and prospects of peptide-based biomaterials. We focus on both chemically synthesized and genetically encoded peptides, including poly-amino acids, elastin-like polypeptides, silk-like polymers and other biopolymers based on repetitive peptide motifs. Applications of these engineered biomolecules in protein purification, controlled drug delivery, tissue engineering, and biosurface engineering are discussed.

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Section: Applications Of Elp-based Protein Purification-as the Princimentioning

confidence: 99%

Peptide-based biopolymers in biomedicine and biotechnology

Chow

Nunalee

Lim

et al. 2008

Materials Science and Engineering: R: Reports

286

231

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show abstract

“…9,10 Recently, applications of these protein polymers have been expanded to stimuli-responsive silk-elastin-like protein block copolymers for high-throughput protein assays, [11][12][13] tunable biopolymers for heavy metal removal, 14 and wheat seed storage proteins. 15 For this reason, we may anticipate that a variety of protein polymers with specific physical properties will be produced for diverse purposes in the future.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Glutamine Deamidation in a Long, Repetitive Protein Polymer via Bioconjugate Capillary Electrophoresis

2004

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We describe a novel method for the determination of glutamine deamidation in a long protein polymer via bioconjugate capillary electrophoresis. Since the current best technique for detection of glutamine (or asparagine) deamidation is mass spectrometry, it is practically impossible to precisely detect the degree of deamidation (i.e., how many residues are deamidated in a polypeptide) in a large protein containing a significant number of glutamine (or asparagine) residues, because the mass difference between native and deamidated residues is just 1 atomic mass unit. However, by covalently attaching polydisperse protein polymers (337 residues) to a monodisperse DNA oligomer (22 bases), the degree of glutamine deamidation, which could not be determined accurately by mass spectrometry, was resolved by free-solution capillary electrophoresis. Electrophoretic separations were carried out after different durations of exposure of the protein to a cyanogen bromide cleavage reaction mixture, which is a general treatment for the purpose of removing an oligopeptide affinity purification tag from fusion proteins. For protein polymers with increasing extents of deamidation, the electromotive force of DNA + polypeptide conjugate molecules increases due to the introduced negative charge of deamidated glutamic acid residues, and consequently CE analysis reveals increasing differences in the electrophoretic mobilities of conjugate molecules, which qualitatively shows the degree of deamidation. Peak analysis of the electropherograms enables quantitative determination of the first four deamidations in a protein polymer. A first-order rate constant of 0.018 h -1 was determined for the deamidation of a single glutamine residue in the protein polymer during the cyanogen bromide cleavage reaction.

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“…The use of ELP as a fusion partner is still a work in progress, as the ELP fusion proteins have reduced overall expression and cause reduced cell growth. 29,[94][95][96] However, in 2012, Liu et al 29 developed an approach that incorporated a mini intein self-cleavage domain (that was fused to the target protein) to facilitate affinity tag removal, along with separately expressed ELP that contained a capture domain for the affinity tag (Figure 2). The affinity pair that was used in this purification technique was a naturally occurring cohesion-dockerin (Coh-Doc) from Clostridium thermocellum that mediates Ca 2+ -dependent binding.…”

Section: Advances In Non-chromatographic Methodsmentioning

confidence: 99%

Technology advancements in antibody purification

Murphy¹,

Devine²,

O’Kennedy³

2016

ANTI

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Abstract:The separation of antibodies from complex mixtures can be achieved using chromatographic or non-chromatographic techniques. The purification of antibodies using chromatography involves the separation of antibodies or antibody-derived molecules present in complex mixtures by passing them through a solid phase (eg, silica resin or beads, monolithic columns, or cellulose membranes) and allowing the antibodies to bind or pass through depending on whether "bind-and-elute" or "flow-through" chromatographic methods are employed. Chromatographic methodologies can incorporate different separation techniques, such as affinity-tag binding, ion-exchange, size-exclusion chromatography, or immunoaffinity chromatography. However, in a concerted effort to become less reliant on chromatography-based separations owing to the high cost of large-scale production, non-chromatographic-based techniques such as precipitation, flocculation, crystallization, filtration, and aqueous two-phase partitioning are now becoming more popular. This review details current chromatographic and non-chromatographic methodo logies used for the purification of antibodies and expands on technological advancements and practical uses that have recently been reported.

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Tunable Biopolymers for Heavy Metal Removal

Cited by 104 publications

References 21 publications

Peptide-based biopolymers in biomedicine and biotechnology

Peptide-based biopolymers in biomedicine and biotechnology

Characterization of Glutamine Deamidation in a Long, Repetitive Protein Polymer via Bioconjugate Capillary Electrophoresis

Technology advancements in antibody purification

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