tetano
Editor, Senior Moderator
Anal Chim Acta. 2014 May 30;828:61-9. doi: 10.1016/j.aca.2014.04.021. Epub 2014 Apr 15.
Substituent effects on the binding of natural product anthocyanidin inhibitors to influenza neuraminidase with mass spectrometry.
Swaminathan K1, M?ller P1, Downard KM2.
Author information
Abstract
The binding of three closely related anthocyanins within the 430-cavity of influenza neuraminidase is studied using a combination of mass spectrometry and molecular docking. Despite their similar structures, which differ only in the number and position of the hydroxyl substituents on the phenyl group attached to the chromenylium ring, subtle differences in their binding characteristics are revealed by mass spectrometry and molecular docking that are in accord with their inhibitory properties by neuraminidase inhibition assays. The cyanidin and delphinidin, with the greatest number of hydroxyl groups, bind more strongly and are better inhibitors than pelargonidin that contains a lone hydroxyl group at the 4' position. The study demonstrates, for the first time, the sensitivity of the mass spectrometry based approach for investigating the molecular basis and relative affinity of antiviral inhibitors, with subtly different structures, to their target protein. It has broader application for the screening of other protein interactions more generally with reasonable high-throughput.
Copyright ? 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
Anthocyanidin, Influenza, Inhibitor, MALDI, Mass spectrometry, Neuraminidase
PMID:
24845816
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24845816
Substituent effects on the binding of natural product anthocyanidin inhibitors to influenza neuraminidase with mass spectrometry.
Swaminathan K1, M?ller P1, Downard KM2.
Author information
Abstract
The binding of three closely related anthocyanins within the 430-cavity of influenza neuraminidase is studied using a combination of mass spectrometry and molecular docking. Despite their similar structures, which differ only in the number and position of the hydroxyl substituents on the phenyl group attached to the chromenylium ring, subtle differences in their binding characteristics are revealed by mass spectrometry and molecular docking that are in accord with their inhibitory properties by neuraminidase inhibition assays. The cyanidin and delphinidin, with the greatest number of hydroxyl groups, bind more strongly and are better inhibitors than pelargonidin that contains a lone hydroxyl group at the 4' position. The study demonstrates, for the first time, the sensitivity of the mass spectrometry based approach for investigating the molecular basis and relative affinity of antiviral inhibitors, with subtly different structures, to their target protein. It has broader application for the screening of other protein interactions more generally with reasonable high-throughput.
Copyright ? 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
Anthocyanidin, Influenza, Inhibitor, MALDI, Mass spectrometry, Neuraminidase
PMID:
24845816
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24845816