The application of MALDI TOF MS in biopharmaceutical research.

Autor: Kafka AP; School of Pharmacy, University of Otago, PO Box 56, Dunedin 9054, New Zealand. alexandra.kafka@coriolis-pharma.com, Kleffmann T, Rades T, McDowell A
Jazyk: angličtina
Zdroj: International journal of pharmaceutics [Int J Pharm] 2011 Sep 30; Vol. 417 (1-2), pp. 70-82. Date of Electronic Publication: 2010 Dec 13.
DOI: 10.1016/j.ijpharm.2010.12.010
Abstrakt: The development and quality assessment of modern biopharmaceuticals, particularly protein and peptide drugs, requires an array of analytical techniques to assess the integrity of the bioactive molecule during formulation and administration. Mass spectrometry is one of these methods and is particularly suitable for determining chemical modifications of protein and peptide drugs. The emphasis of this review is the identification of covalent interactions between protein and peptide bioactives with polymeric pharmaceutical formulations using mass spectrometry with the main focus on matrix-assisted laser desorption/ionization (MALDI) coupled tandem time-of-flight (TOF/TOF) mass spectrometry (MS). The basics of MALDI TOF MS and collision-induced dissociation (CID)-based ion fragmentation will be explained and applications for qualitative characterization of protein and peptide drugs and their interactions with pharmaceutical polymers will be discussed using three case studies.
(Copyright © 2011 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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