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Intensity fading MALDI mass spectrometry

From Wikipedia, the free encyclopedia

Intensity-fading MALDI is a term coined to rename an existing method originally reported in 1999 to indirectly study a Protein–protein interaction or other protein complex[1] and the same year applied to a biological mixture to study the antigenicity of the influenza virus.[2] It involves treating a protein and a potential binding partner with a site-specific endoproteinase with the binding sites identified by their reduced area (or intensity) in a MALDI mass spectrum compared to that of non-bound protein control. It was falsely reported as new and novel in a later application by a Spanish group. The true origins of the approach and a range of applications including those employing gel based separations, drug-protein interactions and the relative affinity of such interactions, are described in a review article.[3]

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  1. ^ Kiselar, Janna G.; Downard, Kevin M. (1999). "Direct Identification of Protein Epitopes by Mass Spectrometry without Immobilization of Antibody and Isolation of Antibody-Peptide Complexes". Analytical Chemistry. 71 (9): 1792–1801. doi:10.1021/ac9811120. PMID 10330909.
  2. ^ Kiselar, Janna G.; Downard, Kevin M. (1999). "Antigenic surveillance of the influenza virus by mass spectrometry". Biochemistry. 38 (43): 14185–14191. doi:10.1021/bi991609j. PMID 10571992.
  3. ^ Downard, Kevin M. (2016). "Indirect study of non-covalent protein complexes by MALDI mass spectrometry: Origins, advantages, and applications of the "intensity-fading" approach". Mass Spectrometry Reviews. 35 (5): 559–573. Bibcode:2016MSRv...35..559D. doi:10.1002/mas.21480. PMID 26250984.