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Scientific article
English

Hydrophobic interaction chromatography for the characterization ofmonoclonal antibodies and related products

Publication date2016
Abstract

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

Keywords
  • Hydrophobic interaction chromatography
  • Antibody-drug-conjugate
  • Therapeutic antibody
  • Method development
  • Columnsa
Citation (ISO format)
FEKETE, Szabolcs et al. Hydrophobic interaction chromatography for the characterization ofmonoclonal antibodies and related products. In: Journal of pharmaceutical and biomedical analysis, 2016, vol. 130, p. 3–18.
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Article (Published version)
accessLevelRestricted
Identifiers
ISSN of the journal0731-7085
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Technical informations

Creation10/17/2016 3:03:00 PM
First validation10/17/2016 3:03:00 PM
Update time03/15/2023 12:50:52 AM
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