Retention in hydrophobic interaction chromatography and dissolution of nonpolar gases in water

Vailaya, Anant; Horváth, Csaba

doi:10.1016/s0301-4622(96)02183-7

Cited by 17 publications

(35 citation statements)

References 31 publications

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“…For pure substances, k A g and k AE g can be readily evaluated from their vaporization [91] and liquid dissolution [52] data. k AE g depends on the property of the eluent as well as the ratio of the eluite to the eluent molecular radii, while k A g depends on the property of the eluite.…”

Section: Fundamentals Of Reversed Phase Chromatography 985mentioning

confidence: 99%

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Fundamentals of Reversed Phase Chromatography: Thermodynamic and Exothermodynamic Treatment

Vailaya

2005

Journal of Liquid Chromatography & Related Technologies

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Reversed phase chromatography (RPC) is the most popular branch of HPLC for the analysis and purification of a wide variety of substances. Despite significant advances in both our knowledge and understanding of the fundamental principles governing the retention behavior in RPC, there is considerable debate in the literature regarding the mechanism of retention. This review addresses the theoretical foundation of the chromatographic technique, with an emphasis on thermodynamic and exothermodynamic treatment of retention equilibrium, as well as their implication on the mechanistic aspects of RPC retention. A unified and rigorous treatment based on the solvophobic theory is reviewed in terms of its ability to shed light on the physicochemical underpinnings of the retention in RPC, and to quantitatively predict the retention behavior of nonpolar compounds, acids and bases, and peptides and proteins. Also highlighted are areas of future challenges in the theory and practice of RPC, potentially leading to a better quantitative understanding and use of the popular technique. It is undoubtedly the unsung champion of the modern biological sciences, enabling the intricacies of cellular biology to be at last discriminated in detail. [2] Without the recent advances in HPLC, modern biology, functional genomics, and proteomics would not exist. The incredible power of HPLC to discern the molecular diversity of biological phenomena is largely attributed to its ability to distinguish mass differences as little as 1 Da in a macromolecule, such as proteins when coupled with mass spectrometry, [3,4] to separate proteins that differ by only a single amino acid, [5] to separate conformational isomers of a long chain polypeptide, [6] and to resolve the different tertiary conformational structures of DNA fragments. [7] The exquisite sensitivity, the speed, and the impressive resolving power of modern HPLC find application in various fields, such as pharmaceutical, food and clinical analysis, pollution control, downstream processing, measurement of physicochemical properties of drugs as well as the separation of peptides, proteins, and nucleic acids. At the heart of the HPLC revolution is the mode of separation that we are all familiar with-reversed phase chromatography (RPC). The seminal works of Horváth and co-workers [8 -11] have contributed significantly to the theory and practice of RPC, resulting in its wide acceptance by the scientific community as a high resolution separation technique of choice. It is estimated that approximately 80% of HPLC analysis is conducted in this mode. [12] The success of this technique is attributed to the employment of microparticulate alkyl-silica monomeric bonded phases, such as octadecylated silica, which offers high separation efficiency combined with unparalleled convenience, versatility and reproducibility. The use of bonded hydrocarbonaceous stationary phases having a variety of functional groups and a wide choice of hydroorganic eluents to modulate retention offer a broad range of operating con...

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Section: Fundamentals Of Reversed Phase Chromatography 985mentioning

confidence: 99%

“…[52] It is therefore of interest to measure such parameters in RPC Figure 9. It is an important physicochemical parameter that characterizes processes driven by the hydrophobic effect.…”

Section: Prediction Of Hydrophobic Selectivitymentioning

confidence: 99%

Fundamentals of Reversed Phase Chromatography: Thermodynamic and Exothermodynamic Treatment

Vailaya

2005

Journal of Liquid Chromatography & Related Technologies

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“…Elucidation of the nature of the dehydration processes that the sorbent and protein or polypeptide undergo upon association is of great importance for elaborating the biophysical basis of liquid chromatographic separations. When the interactive behaviour of proteins and polypeptides is viewed in this manner, these results can be mechanistically equated with the findings obtained, for example, by Vailaya and Horvath 23,24,28 for the retention of dansyl amino acids to hydrophobic sorbents or other processes based on hydrophobic interactions such as the dissolution of low molecular weight non-polar organic compounds in water. In all of these phenomena, changes in the structure of water play a major role-if not the dominant role-in the hydration/de-hydration processes with the entropy gain of the system also contributed by the ions, solvents or other molecules present in the system.…”

Section: Protein Purification Achieved By Liquid Chromatography Accormentioning

confidence: 75%

Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography

Lin

Chen

Hearn

2002

J of Molecular Recognition

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“…The temperature effect on HIC performance has been studied by many authors [61,62,71,[74][75][76]. Vailaya and Horvath [76] established the existence of exothermodynamic relationships (enthalpy-entropy compensation) in the HIC process.…”

Section: Temperature Effectmentioning

confidence: 99%

“…Vailaya and Horvath [76] established the existence of exothermodynamic relationships (enthalpy-entropy compensation) in the HIC process. Large and positive enthalpy and entropy changes were observed at low temperatures, which decrease with an increase in temperature.…”

Section: Temperature Effectmentioning

confidence: 99%

Current insights on protein behaviour in hydrophobic interaction chromatography

Lienqueo

Mahn

Salgado

et al. 2007

Journal of Chromatography B

100

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Retention in hydrophobic interaction chromatography and dissolution of nonpolar gases in water

Cited by 17 publications

References 31 publications

Fundamentals of Reversed Phase Chromatography: Thermodynamic and Exothermodynamic Treatment

Fundamentals of Reversed Phase Chromatography: Thermodynamic and Exothermodynamic Treatment

Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography

Current insights on protein behaviour in hydrophobic interaction chromatography

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