Flow Lectin Affinity Chromatography−A Model with Sambucus nigra Agglutinin

Silva, M Luísa S; Gomes, Catarina; Garcia, M Beatriz Quinaz

doi:10.4172/2168-958x.1000121

Cited by 4 publications

(3 citation statements)

References 30 publications

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“…Lectins are glycan-binding proteins that are widely distributed in nature and have diverse important functions on cells, such as agglutination, redistribution of cell surface components, toxicity, modification of the activity of membrane enzymes, cell aggregation, and immunomodulation. − Lectins have recently been used to successfully detect cancer biomarkers in tissues and complex fluids . Many lectins have been applied in several medical research areas, such as drug delivery, , inhibition of cancer cell adhesion, inhibition of cancer cell growth, and biomarkers for disease detection and monitoring, due to their carbohydrate binding specificities. Currently, cancer biomarker discovery is an important field of research, since only a few biomarkers are available for use in clinical settings .…”

Section: Introductionmentioning

confidence: 99%

“…[4][5][6][7] Lectins have recently been used to successfully detect cancer biomarkers in tissues and complex fluids. 13 Many lectins have been applied in several medical research areas, such as drug delivery 16,17 , inhibition of cancer cell adhesion 18 , inhibition of cancer cell growth 19 , and biomarkers for disease detection and monitoring 13 , due to their carbohydrate binding specificities. Currently, cancer biomarker discovery is an important field of research, since only a few of thembiomarkers are frequently being usedavailable for use in the clinical settings.…”

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confidence: 99%

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Design of Thermoresponsive Elastin-Like Glycopolypeptides for Selective Lectin Binding and Sorting

et al. 2020

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Selective lectin binding and sorting was achieved using thermosensitive recombinant elastin-like polypeptide (ELP) glycoconjugates in simple centrifugation-precipitation assays. A recombinant ELP, (VPGXG) 40 , was designed to contain periodically spaced methionine residues to enable chemoselective post-synthesis modification via thioether alkylation using alkyne functional epoxides. The resulting sulfonium groups were selectively demethylated to give alkyne functionalized homocysteine residues, which were then conjugated with azido-functionalized monosaccharides to obtain ELP glycoconjugates with periodic saccharide functionality. These modifications were also found to allow modulation of ELP temperature dependent water solubility. The multivalent ELP glycoconjugates were evaluated for specific recognition, binding and separation of the lectin Ricinus communis agglutinin (RCA 120) from a complex protein mixture. RCA 120 and ELP glycoconjugate interactions were evaluated using laser scanning confocal microscopy and dynamic light scattering measurements. Due to the thermoresponsive nature of the ELP glycoconjugates, it was found that heating a mixture of galactosefunctionalized ELP and RCA 120 in complex media selectively yielded a phase 1 separated pellet of the ELP-RCA 120 complexes. Based on these results, ELP glycoconjugates show promise as designer biopolymers for selective protein binding and sorting.

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

Design of Thermoresponsive Elastin-Like Glycopolypeptides for Selective Lectin Binding and Sorting

et al. 2020

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“…Neu5Acα2-6Gal(NAc)-R N-and O-linked Shibuya et al, 1987;Silva et al, 2017 Gorse or furze (Ulex europaeus) seed agglutinin-I…”

Section: Snamentioning

confidence: 99%

Lectins: an effective tool for screening of potential cancer biomarkers

Hashim

Jayapalan

Lee

2017

Preprint

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Electrochemical Analysis of Glycoprotein Samples Prepared on a Pneumatically‐controlled Microfluidic Device

2019

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In this work, we designed and manufactured a microfluidic device for isolation and purification of glycoprotein samples. The conceived sample preparation device was fabricated in polycarbonate by micro‐milling. The flow control and the fluid dosage into the micro‐channels was solved by equipping the device with integrated pneumatic valves. The biochemical functionality was provided by beaded support modified by molecules with affinity to glycoproteins which was stacked inside the micro‐channel reminiscent of packed affinity columns used in glycoprotein lectin assays. Unlabeled glycoproteins, namely fetuin, asialofetuin, and prostate‐specific antigen, were voltammetrically analyzed using catalytic peak H at silver amalgam electrode.

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Flow Lectin Affinity Chromatography−A Model with Sambucus nigra Agglutinin

Cited by 4 publications

References 30 publications

Design of Thermoresponsive Elastin-Like Glycopolypeptides for Selective Lectin Binding and Sorting

Design of Thermoresponsive Elastin-Like Glycopolypeptides for Selective Lectin Binding and Sorting

Lectins: an effective tool for screening of potential cancer biomarkers

Electrochemical Analysis of Glycoprotein Samples Prepared on a Pneumatically‐controlled Microfluidic Device

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