Hydrophobic Interaction Chromatography: Fundamentals and Applications in Biomedical Engineering

Mahn, Andrea

doi:10.5772/18045

Cited by 2 publications

(1 citation statement)

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“…HIC is a widely used approach for protein purifications [15,67,68,69,70]. In this review, we focus only on analytical scale separations and mAbs/ADCs applications.…”

Section: Application Of Hic For Protein Separationsmentioning

confidence: 99%

Hydrophobic interaction chromatography for the characterization of monoclonal antibodies and related products

Fekete

Veuthey

Beck³

et al. 2016

Journal of Pharmaceutical and Biomedical Analysis

121

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Hydrophobic interaction chromatography (HIC) is a historical strategy used for the analytical purification and characterization of proteins. Similarly to what can be done in reversed-phase liquid chromatography (RPLC), HIC is able to separate protein species based on their hydrophobicity, but using different conditions. Compared to RPLC, the main benefit of HIC is its ability to perform separations under non denaturing conditions (i.e. physiological pH conditions, ambient mobile phase temperature and no need for organic solvents) and so an orthogonal method. The goal of this review is to provide a general overview of theoretical and practical aspects of modern HIC applied for the characterization of therapeutic protein biopharmaceuticals including monoclonal antibodies (mAbs), antibody drug conjugates (ADCs) and bispecific antibodies (bsAbs). Therefore, method development approaches, state-of-the-art column technology, applications and future perspectives are described and critically discussed.

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“…HIC is a widely used approach for protein purifications [15,67,68,69,70]. In this review, we focus only on analytical scale separations and mAbs/ADCs applications.…”

Section: Application Of Hic For Protein Separationsmentioning

confidence: 99%