Adsorption and Surface Properties of Vladipor Cellulose Acetate and Polysulfonamide Membranes

Khokhlova, Tatiana D.; Dzyubenko, V. G.; Березкин, В. В.; Bon, A. I.; Pervov, N. V.; Shishova, I. I.; Dubyaga, V.P.; Mchedlishvili, B. V.

doi:10.1007/s10595-005-0161-x

Cited by 6 publications

(4 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The ccc isoform was eluted at an effective modifier content of 12.9% acetonitrile and 11.7% isopropanol, respectively, hence they possess similar elution strengths (see the Supporting Information for chromatograms). Both, acetonitrile 32 and isopropanol 33 are known to suppress hydrophobic interactions, which in turn must be involved in the binding mechanism, particularly in the interaction with the ccc isoform, because no topoisomer selectivity was observed in this case. Although the chromatographic resolution was reasonable when using isopropanol (R oc/lin = 0.25, R lin/ccc = 1.17) or acetonitrile (R oc/lin = 0.35, R lin/ccc = 1.73), we found that pDNA was not eluted quantitatively from the column.…”

Section: ■ Materials and Methodsmentioning

confidence: 98%

Chemoaffinity Material for Plasmid DNA Analysis by High-Performance Liquid Chromatography with Condition-Dependent Switching between Isoform and Topoisomer Selectivity

et al. 2013

View full text Add to dashboard Cite

Plasmid DNA may exist in three isoforms, the linear, open-circular (oc, "nicked"), and covalently closed circular (ccc, "supercoiled") form. We have recently reported on the chromatographic separation of supercoiled plasmid topoisomers on cinchona-alkaloid modified silica-based stationary phases. Herein, we present a selectivity switching mechanism to achieve separation of isoforms and/or supercoiled topoisomers using the very same chromatographic column and system. While salt gradient elution facilitates topoisomer separation, the supercoiled species are eluting as a single peak upon elution by a mixed pH and organic modifier gradient, still well separated from the other isoforms. We have found that a mobile phase pH value near the pI of the zwitterionic adsorbent surface leads to full recovery of all plasmid DNA isoforms, which is a major issue when using anion exchange-based resins. Furthermore, the observed elution pattern, oc < linear < ccc, is constant upon changes of mobile phase composition, gradient slope, and plasmid size. The remarkable isoform selectivity found on quinine-based selectors is explained by van't Hoff plots, revealing a different binding mechanism between the supercoiled plasmid on one hand and the oc and linear isoforms on the other hand.

show abstract

Section: ■ Materials and Methodsmentioning

confidence: 98%

Chemoaffinity Material for Plasmid DNA Analysis by High-Performance Liquid Chromatography with Condition-Dependent Switching between Isoform and Topoisomer Selectivity

et al. 2013

View full text Add to dashboard Cite

show abstract

“…So it is usually used as a film base in photography (Fujf, 2003) and as a component in adhesives (Ilicheva, Feldman, & Nikolskii, 1997). Furthermore, it can also be used as reverse osmosis (Bodalo, Gomez, Gomez, Leon, & Tejera, 2005;Khokhlova et al, 2005) and nanofiltration membranes (Choi, Fukushi, & Yamamoto, 2007). Grafted with functional groups such as -COOH, -SO 3 H and -NH 2 groups, CA can bond with heavy metal ions through surface complexation mechanisms (Liu & Bai, 2006).…”

Section: Introductionmentioning

confidence: 99%

Electrospun membrane of cellulose acetate for heavy metal ion adsorption in water treatment

Tian

Liu

et al. 2011

Carbohydrate Polymers

255

109

View full text Add to dashboard Cite

“…Protein adsorption on charged surfaces plays a role in a number of fields such as biomaterials (Wittmer et al, 2007), diagnostics (Bilitewski, 2006), and bioseparations (Khokhlova et al, 2005). Protein adsorption in ion exchange chromatographic systems is of particular importance for the production of biopharmaceuticals.…”

Section: Introductionmentioning

confidence: 99%

Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library

Chung¹,

Hou²,

Freed³

et al. 2008

Biotech & Bioengineering

View full text Add to dashboard Cite

A library of cold shock protein B (CspB) mutant variants was employed to study protein binding affinity and preferred orientations in cation exchange chromatography. Single site mutations introduced at charged amino acids on the protein surface resulted in a homologous protein set with varying charge density and distribution. The retention times of the mutants varied significantly during linear gradient chromatography. While the expected trends were observed with increasing or decreasing positive charge on the protein surface, the degree of change was a strong function of the location and microenvironment of the mutated amino acid. Quantitative structure-property relationship (QSPR) models were generated using a support vector regression technique that was able to give good predictions of the retention times of the various mutants. Molecular descriptors selected during model generation were used to elucidate the factors affecting protein retention. Electrostatic potential maps were also employed to provide insight into the effects of protein surface topography, charge density and charge distribution on protein binding affinity and possible preferred binding orientations. The use of this protein mutant library in concert with the qualitative and quantitative analyses presented in the article provides an improved understanding of protein behavior in ion exchange systems.

show abstract

Adsorption and Surface Properties of Vladipor Cellulose Acetate and Polysulfonamide Membranes

Cited by 6 publications

References 2 publications

Chemoaffinity Material for Plasmid DNA Analysis by High-Performance Liquid Chromatography with Condition-Dependent Switching between Isoform and Topoisomer Selectivity

Chemoaffinity Material for Plasmid DNA Analysis by High-Performance Liquid Chromatography with Condition-Dependent Switching between Isoform and Topoisomer Selectivity

Electrospun membrane of cellulose acetate for heavy metal ion adsorption in water treatment

Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library

Contact Info

Product

Resources

About