Chromatographic probing of protein-sorbent interactions

Lesin, Viesturs; Ruckenstein, Eli

doi:10.1016/0021-9797(89)90270-1

Cited by 15 publications

(5 citation statements)

References 28 publications

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“…Proteins generally elute in order of increasing isoelectric points, with the exception of cytochrome c , which eluted after other proteins with higher isoelectric points. This may be due, in part, to a concentration of basic amino acids in a localized area on this protein's surface 1 Gradient elution separation of cationic proteins on PEZ.…”

Section: Resultsmentioning

confidence: 99%

Chromatographic Characterization of Phosphonate Analog EDTA-Modified Zirconia Support for Biochromatographic Applications

Clausen

Carr

1998

Anal. Chem.

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Zirconium dioxide (zirconia) has a great affinity for inorganic and organic phosphate. Previous work from this laboratory demonstrated the utility of phosphate-modified microparticulate zirconia as a support for protein separations. We have extended this investigation to include the study of ethylenediamine-N,N'-tetramethylphosphonic acid (EDTPA), a phosphonate analog of EDTA, as a surface modifier for zirconia. Our work explores the use of EDTPA-modified zirconia (PEZ) for its potential use as a high-performance inorganic cation-exchange support for the separation of proteins. The phosphate groups in EDTPA very effectively block the sites responsible for strong interactions of hard Lewis bases with zirconia's surface. Modification of zirconia with EDTPA provides a "biocompatible" stationary phase, resulting in high mass recoveries of proteins. We compare PEZ with inorganic phosphate-modified zirconia to show increased efficiency, as well as unique selectivities for chromatography of proteins on the chelator-modified surface. Finally, the selectivity, efficiency, and separation mechanism are reported. The studies show that PEZ is a useful high-performance ion-exchange support for the separation of cationic proteins and for modulating the sites responsible for the high affinity of zirconia toward certain classes of anions.

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Section: Resultsmentioning

confidence: 99%

Chromatographic Characterization of Phosphonate Analog EDTA-Modified Zirconia Support for Biochromatographic Applications

Clausen

Carr

1998

Anal. Chem.

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“…a-Chymotrypsinogen A was chosen as the model system for the adsorption studies since its three-dimensional structure has been elucidated36 37 and its adsorption behavior on other substrates has been documented by several different techniques. [38][39][40][41] The enzyme consists of a single polypeptide chain with 245 amino residues. It is a relatively small, globular protein cross-linked by five disulfide bonds.…”

Section: Resultsmentioning

confidence: 99%

Acoustic network analysis as a novel technique for studying protein adsorption and denaturation at surfaces

Yang¹,

Chung²,

Thompson³

1993

Anal. Chem.

103

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The understanding of the interaction of proteins with solid surfaces1-3 is important in the development of implantable medical devices, biotechnology, and biosensors. Some of the more common techniques for studying proteins at an interface include radiolabeling and fluorescent tagging; spectroscopic methods such as ellipsometry, total internal reflectance fluorescence (TIRF), and attenuated total reflectance Fouriertransform infrared spectroscopy (ATR-FTIR); and surface characterization methods such as X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM). These techniques have been thoroughly reviewed.* 1 They provide information either on the amount and rate of adsorption of proteins or on the conformation of the adsorbate.However, protein adsorption and the orientation of the adsorbed molecules involves a large number of time-dependent dynamic phenomena where conformational changes can occur during the adsorption process. Few of the above techniques are capable of monitoring in situ adsorption and providing evidence of conformational effects in real time. In this preliminary report, we demonstrate that the response of the thickness-shear mode (TSM) acoustic wave sensor can be correlated to interfacial processes involving protein adsorption and denaturation at surfaces.A number of studies have employed the so-called quartz crystal microbalance technique to determine the amount of adsorbed protein.4-7 The detection scheme is based on the changes of the oscillating frequency of piezoelectric devices upon mass loading.8 The mass-frequency relationship is describe by the Sauerbrey equation 2/02Am A(pqMq)1/2

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“…For example, based on early experimental results [85,86], Feng and Ruckenstein [43] examined the adsorption of a specific polyampholyte chain on a single spherical nano-particle with three different radii. In this application, the charge density at the particle surface regulates the strength of the adsorption field (corresponding to our parameter ǫ) and the polymer composition regulates the location of the coil-globule transition (corresponding to ǫ LJ ).…”

Section: Discussionmentioning

confidence: 99%

Polymer adsorption on curved surfaces

Arkin

Janke

2017

Phys. Rev. E

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The conformational behavior of a coarse-grained finite polymer chain near an attractive spherical surface was investigated by means of multicanonical Monte Carlo computer simulations. In a detailed analysis of canonical equilibrium data over a wide range of sphere radius and temperature, we have constructed entire phase diagrams both for nongrafted and end-grafted polymers. For the identification of the conformational phases, we have calculated several energetic and structural observables such as gyration tensor based shape parameters and their fluctuations by canonical statistical analysis. Despite the simplicity of our model, it qualitatively represents in the considered parameter range real systems that are studied in experiments. The work discussed here could have experimental implications from protein-ligand interactions to designing nanosmart materials.

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Chromatographic probing of protein-sorbent interactions

Cited by 15 publications

References 28 publications

Chromatographic Characterization of Phosphonate Analog EDTA-Modified Zirconia Support for Biochromatographic Applications

Chromatographic Characterization of Phosphonate Analog EDTA-Modified Zirconia Support for Biochromatographic Applications

Acoustic network analysis as a novel technique for studying protein adsorption and denaturation at surfaces

Polymer adsorption on curved surfaces

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