tetano
Editor, Senior Moderator
Anal Chem. 2012 Mar 12. [Epub ahead of print]
Anti-Viral Inhibitor Binding to Influenza Neuraminidase by MALDI Mass Spectrometry.
Swaminathan K, Downard KM.
Abstract
A MALDI mass spectrometry based approach is applied to identify active site domains within influenza neuraminidase that bind the anti-viral inhibitors zanamivir (ZANA) and 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (DANA). Combined data from the tryptic and Glu-C endoproteinase digests of neuraminidase-inhibitor complexes have identified binding peptides that contain the active site residues Arg118, Glu119, Arg156, Glu276 and Tyr406. The binding of these residues was confirmed from the analysis of available X-ray crystal structures. The ability to identify peptides within the active sites of proteins and likely binding residues provides both a rapid and relatively high throughput approach with which to screen protein-drug interactions by MALDI mass spectrometry.
PMID:
22409142
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22409142
Anti-Viral Inhibitor Binding to Influenza Neuraminidase by MALDI Mass Spectrometry.
Swaminathan K, Downard KM.
Abstract
A MALDI mass spectrometry based approach is applied to identify active site domains within influenza neuraminidase that bind the anti-viral inhibitors zanamivir (ZANA) and 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (DANA). Combined data from the tryptic and Glu-C endoproteinase digests of neuraminidase-inhibitor complexes have identified binding peptides that contain the active site residues Arg118, Glu119, Arg156, Glu276 and Tyr406. The binding of these residues was confirmed from the analysis of available X-ray crystal structures. The ability to identify peptides within the active sites of proteins and likely binding residues provides both a rapid and relatively high throughput approach with which to screen protein-drug interactions by MALDI mass spectrometry.
PMID:
22409142
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22409142