Binding of antibodies to concanavalin A-modified monolithic cryogel

Babaç, Ceyhun; Yavuz, Handan; Galaev, Igor Yu.; Pi̇şki̇n, Erhan; Deni̇zli̇, Adil

doi:10.1016/j.reactfunctpolym.2006.03.007

Cited by 104 publications

(51 citation statements)

References 44 publications

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“…Cryogels with their macroporous structure facilitating mass-transport of large molecules can be a good alternative to overcome these problems. [12][13][14] Recently, several studies had been published for depletion of Hb based on the molecular recognition method. [15][16][17][18] In addition to the acrylamide based monomers, Zhao et al showed that novel functional monomers might be attractive for promoting specific protein interactions with binding sites of polymer networks.…”

Section: Introductionmentioning

confidence: 99%

Molecularly Imprinted PHEMA‐Based Cryogel for Depletion of Hemoglobin from Human Blood

Derazshamshir

Baydemir

Andaç

et al. 2010

Macro Chemistry & Physics

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A new generation of molecularly imprinted macroporous hydrogels, so‐called cryogels, were prepared for depletion of hemoglobin from human blood. Hb‐PHEMAH cryogels were prepared with gel fraction yields up to 90%, and its morphology and porosity were characterized by FTIR, SEM, swelling studies, flow dynamics and surface area measurements. Selective binding experiments were performed in the presence of competitive proteins Myb and BSA. Hb‐PHEMAH cryogel exhibited a high binding capacity and selectivity for Hb in the presence of Myb and BSA. The selectivity of Hb‐PHEMAH cryogel for Hb was confirmed by HPLC. Hb depletion from blood hemolysate was also studied using SDS‐PAGE. Hb‐PHEMAH cryogel can be reused many times with no apparent decrease in Hb adsorption capacity.magnified image

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Section: Introductionmentioning

confidence: 99%

Molecularly Imprinted PHEMA‐Based Cryogel for Depletion of Hemoglobin from Human Blood

Derazshamshir

Baydemir

Andaç

et al. 2010

Macro Chemistry & Physics

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“…However, in spite of its high selectivity, protein A has some drawbacks such as its high cost and the difficulty to immobilize it in the proper orientation (Denizli and Arica, 2000). To overcome such drawbacks, affinity-binding techniques that utilize concanavalin A (Con A), instead of protein A, have become promising candidates due to the ability of Con A to recognize the carbohydrate moiety of the IgG molecule (Babac et al, 2006). Con A is a tetrameric metalloprotein found in the jack bean (Canavalia ensiformis) and can bind to a-glucose and a-mannose with high molecular specificity Gestwicki et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

A multipurpose capacitive biosensor for assay and quality control of human immunoglobulin G

Labib

Hedström

Amin

et al. 2009

Biotech & Bioengineering

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We report a flow-injection biosensor system with a capacitive transducer for assay and quality control of human immunoglobulin G (hIgG). The sensing platform is based on self-assembled monolayers (SAMs) of carboxylic acid terminated alkyl-thiols with covalently attached concanavalin A. The electrochemical characteristics of the sensor surface were assessed by cyclic voltammetry using a permeable redox couple (potassium ferricyanide). The developed biosensor proved capable of performing a sensitive label-free assay of hIgG with a detection limit of 1.0 microg mL(-1). The capacitance response depended linearly on hIgG concentration over the range from 5.0 to 100 microg mL(-1), in a logarithmic plot. Typical measurements were performed in 15 min and up to 18 successive assays were achieved without significant loss of sensitivity using a single electrode. In addition, the biosensor can detect hIgG aggregates with concentrations as low as 0.01% of the total hIgG content (5.0 microg mL(-1)). Hence, it represents a potential post-size-exclusion chromatography-UV (post-SEC-UV) binding assay for in-process quality control of hIgG, which cannot be detected by SEC-UV singly at concentrations below 0.3% of the total hIgG content.

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“…Babac and coworkers employed Con A immobilized on a poly(acrylamide-allyl glycidyl ether) cryogel monolithic column to trap IgG antibodies from an aqueous solution and from human serum [136]. The column continued to trap IgG antibodies even after 10 cycles.…”

Section: Lectins As Affinity Ligandsmentioning

confidence: 99%

Bioaffinity chromatography on monolithic supports

Tetala

Beek

2010

J of Separation Science

115

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Affinity chromatography on monolithic supports is a powerful analytical chemical platform because it allows for fast analyses, small sample volumes, strong enrichment of trace biomarkers and applications in microchips. In this review, the recent research using monolithic materials in the field of bioaffinity chromatography (including immunochromatography) is summarized and discussed. After giving an introduction into affinity chromatography, information on different biomolecules (antibodies, enzymes, lectins, aptamers) that can act as ligands in bioaffinity chromatography is presented. Subsequently, the history of monoliths, their advantages, preparation and formats (disks, capillaries and microchips) as well as ligand immobilization techniques are mentioned. Finally, analytical and preparative applications of bioaffinity chromatography on monoliths are presented. During the last four years 37 papers appeared. Protein A and G are still most often used as ligands for the enrichment of immunoglobulins. Antibodies and lectins remain popular for the analysis of mainly smaller molecules and saccharides, respectively. The highly porous cryogels modified with ligands are applied for the sorting of different cells or bacteria. New is the application of aptamers and phages as ligands on monoliths. Convective interaction media (epoxy CIM disks) are currently the most used format in monolithic bioaffinity chromatography.

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Binding of antibodies to concanavalin A-modified monolithic cryogel

Cited by 104 publications

References 44 publications

Molecularly Imprinted PHEMA‐Based Cryogel for Depletion of Hemoglobin from Human Blood

Molecularly Imprinted PHEMA‐Based Cryogel for Depletion of Hemoglobin from Human Blood

A multipurpose capacitive biosensor for assay and quality control of human immunoglobulin G

Bioaffinity chromatography on monolithic supports

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