Prediction of protein retention at gradient elution conditions in ion-exchange chromatography

Hallgren, Elisabeth

doi:10.1016/s0021-9673(99)00646-9

Cited by 13 publications

(3 citation statements)

References 20 publications

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“…Protein retention time predictions for ion-exchange (IEC) and hydrophobic interaction chromatography (HIC) were the subject of intensive studies. [92][93][94][95][96] These chromatographic methods allow the separation and/or purification of intact proteins under non-denaturing conditions. Also, IEC is often followed by HIC to optimize protein purification.…”

Section: Peptide Retention Prediction For the Alignment Of Lc-ms/ms Runsmentioning

confidence: 99%

“…Hallgren et al described a theoretical approach combining the fundamental equation of gradient elution and the so-called "slab" model for the calculation of protein capacity factors in isocratic separation in IEC. 92 Later, Song et al developed an SVR-based algorithm establishing the quantitative structure-retention relationship for predicting protein retention times in anion-exchange chromatography. 93 Xu et al have attempted to correlate the physicochemical properties of proteins, such as the isoelectric point, molecular weight, and aqueous two-phase partitioning coefficients of model proteins with retention times of cation-exchange chromatography using partial least squares regression.…”

Section: Peptide Retention Prediction For the Alignment Of Lc-ms/ms Runsmentioning

confidence: 99%

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Predictive chromatography of peptides and proteins as a complementary tool for proteomics

Tarasova

Masselon

Gorshkov

et al. 2016

Analyst

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In the last couple of decades, considerable effort has been focused on developing methods for quantitative and qualitative proteome characterization. The method of choice in this characterization is mass spectrometry used in combination with sample separation. One of the most widely used separation techniques at the front end of a mass spectrometer is high performance liquid chromatography (HPLC). A unique feature of HPLC is its specificity to the amino acid sequence of separated peptides and proteins. This specificity may provide additional information about the peptides or proteins under study which is complementary to the mass spectrometry data. The value of this information for proteomics has been recognized in the past few decades, which has stimulated significant effort in the development and implementation of computational and theoretical models for the prediction of peptide retention time for a given sequence. Here we review the advances in this area and the utility of predicted retention times for proteomic applications.

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Section: Peptide Retention Prediction For the Alignment Of Lc-ms/ms Runsmentioning

confidence: 99%

Section: Peptide Retention Prediction For the Alignment Of Lc-ms/ms Runsmentioning

confidence: 99%

Predictive chromatography of peptides and proteins as a complementary tool for proteomics

Tarasova

Masselon

Gorshkov

et al. 2016

Analyst

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“…Models are also being developed to predict the interaction behaviour of proteins, and with it their retention times for a given ion strength value [56]; this type of study was carried out using, among others, several metal-binding proteins such as cytochrome C, carbonic anhydrase, conalbumin and albumin.…”

Section: Principlesmentioning

confidence: 99%

Identification, characterization and determination of metal-binding proteins by liquid chromatography. A review

Guntiñas

Bordin

Rodríguez

2002

Analytical and Bioanalytical Chemistry

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The use of liquid chromatography in the separation and determination of metal-binding proteins is reviewed. Advantages and drawbacks of different chromatographic techniques based on various principles: size exclusion, ion exchange (cationic and ionic), reversed phase and affinity, are presented and discussed. The topic "metal-binding proteins" is considered and presented from two different points of view. The first one regards metal speciation in biological samples (serum and blood). In metal speciation studies, the exact identity of the protein to which the metal is bound often remains unknown. The second point of view is that, frequently, the interest of analyzing metal-binding proteins is not related anymore to the metallic fraction of the protein, but to other chemical structures attached to the protein, such as carbohydrates, which indirectly determine how good the function of the protein is. In this review, special attention is paid to studies dealing with the glycosylation of transferrin, and with the glycated isoform of haemoglobin.

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Recent trends and some applications of isothermal titration calorimetry in biotechnology

Roselin

Lin

et al. 2010

Biotechnology Journal

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Isothermal titration calorimeters (ITCs) are thermodynamic instruments used for the determination of enthalpy changes in any physical/chemical reaction. This can be applied in various fields of biotechnology. This review explains ITC applications, especially in bioseparation, drug development and cell metabolism. In liquid chromatography, the separation/purification of specific proteins or polypeptides in a mixture is usually achieved by varying the adsorption affinities of the different proteins/polypeptides for the adsorbent under different mobile-phase conditions and temperatures. Using ITC analysis, the binding mechanism of proteins with adsorbent solid material is derived by elucidating enthalpy and entropy changes, which offer valuable guidelines for designing experimental conditions in chromatographic separation. The binding affinity of a drug with its target is studied by deriving binding enthalpy and binding entropy. To improve the binding affinity, suitable lead compounds for a drug can be identified and their affinity tested by ITC. Recently ITC has also been used in studying cell metabolism. The heat produced by animal cells in culture can be used as a primary indicator of the kinetics of cell metabolism, which provides key information for drug bioactivity and operation parameters for process cell culture.

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Prediction of protein retention at gradient elution conditions in ion-exchange chromatography

Cited by 13 publications

References 20 publications

Predictive chromatography of peptides and proteins as a complementary tool for proteomics

Predictive chromatography of peptides and proteins as a complementary tool for proteomics

Identification, characterization and determination of metal-binding proteins by liquid chromatography. A review

Recent trends and some applications of isothermal titration calorimetry in biotechnology

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