DMSA-Functionalized Mesoporous Alumina with a High Capacity for Selective Isolation of Immunoglobulin G

Abstract

A novel dimercaptosuccinic acid-functionalized mesoporous alumina (DMSA–MA) is synthesized by the dicarboxylic acid groups of dimercaptosuccinic acid molecules coordinating to the Al3+ ions located in the mesostructure. The as-prepared DMSA–MA composites possess a large surface area of 91.17 m2/g as well as a uniform pore size and a high pore volume of 17.22 nm and 0.23 cm3/g, respectively. DMSA coating of mesostructures significantly enhanced their selectivity for glycoprotein adsorption through a powerful hydrophilic binding force, and the maximum adsorption capacity of immunoglobulin G (IgG) can reach 2298.6 mg g–1. The captured IgG could be lightly stripped from the DMSA–MA composites with an elution rate of 98.3% by using 0.5 wt % CTAB solution as the elution reagent. DMSA–MA is further employed as a sorbent for the enrichment of IgG heavy chain and light chain from human serum sample. SDS–PAGE assay results showed the obtained IgG with high purity compared to that of the standard solution of IgG.

Nanomotor-based adsorbent for blood Lead(II) removal in vitro and in pig models

“…2 C). After DMSA was used for modification, it is difficult to observe the characteristic peaks of sulfhydryl groups by FT-IR spectroscopy [ [53] , [54] , [55] , [56] , [57] ]. Ellman spectrophotometry was used to detect the sulfhydryl content in Fe 3 O 4 @DMSA [ 58 , 59 ].…”

“…The O 1s spectrum at around 529.6 eV and 531.5 eV were corresponded to O–C O and C=O of the carboxyl functional group, respectively. And the new peak at around 530.2 eV after adsorption can be attributed to the formation of Pb–O [ 56 , 81 , 82 ]. In the S 2p spectrum, the peak at around 163.3 eV was the free sulfhydryl functional group, and the peak at around 164.0 eV was the disulfide bond after oxidation in the synthesis process [ 83 , 84 ].…”

Tailoring the Surface Properties of Co-based Metal–Organic Frameworks for Highly Efficient and Selective Enrichment of Immunoglobulin G

“…The adsorbed IgG by Co-MOF-OH could be recovered by using 0.2% ( m / v ) CTAB as the elution reagent, as CTAB can interact with hydrophobic regions of proteins to form a stable micelle system . Circular dichroism (CD) spectra were measured to analyze the IgG recovered from Co-MOF-OH.…”

“…The adsorbed IgG by Co-MOF-OH could be recovered by using 0.2% (m/v) CTAB as the elution reagent, as CTAB can interact with hydrophobic regions of proteins to form a stable micelle system. 33 Circular dichroism (CD) spectra were measured to analyze the IgG recovered from Co-MOF-OH. The CD spectrum of the recovered IgG, after ultrafiltration with a 3 kDa centrifugal filter to remove CTAB, is illustrated in Figure 3c.…”

Boron-Modified Defect-Rich Molybdenum Disulfide Nanosheets: Reducing Nonspecific Adsorption and Promoting a High Capacity for Isolation of Immunoglobulin G

“…The physiological functions include blood coagulation, immunity, secretion, material transport, signal recognition, cell migration, and cell differentiation . In the past few years, several strategies based on solid phase extraction have been applied for glycoproteins/glycopeptides isolation, for example, hydrazine chemistry, lectin affinity, hydrophilic interactions, , and boronic acid chemistry . Among these, boronate affinity materials, − because of their unbiased recognition based on covalent interactions between boronic acid and glycans in alkaline media, − are considered as efficient absorbents in glycoprotein enrichment.…”