©1996-2021 All Rights Reserved. Online
Journal of Bioinformatics .
You may not store these pages in any form except for your own personal use. All
other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the
before mentioned must be gained in writing from the publisher. This
article is exclusively copyrighted in its entirety to OJB publications. This
article may be copied once but may not be, reproduced or re-transmitted without
the express permission of the editors. This journal satisfies the refereeing
requirements (DEST) for the Higher Education Research Data Collection
(Australia). Linking:To link to
this page or any pages linking to this page you must link directly to this page
only here rather than put up your own page.
OJBTM
Online Journal of Bioinformatics©
Volume 20(2):135-143, 2019.
In silico
drug binding glycerol phosphate dehydrogenase-1 for treatment of Brugada syndrome.
Senthil Raja, Raja Rajenderan
Anbazhagan
Bioinformatics Division, Department of Zoology,
Faculty of Science, Annamalai University, India.
Raja S, Anbazhagan RR., In silico drug binding glycerol
phosphate dehydrogenase-1 for treatment of Brugada
syndrome, Onl J Bioinform.,
20(2):135-143,
2019. Brugada
syndrome can be characterized by ECG ST segment elevation in right precordial
leads (V1 to V3), in right bundle branch block, ventricular tachyarrhythmia and
sudden cardiac death. Syncope at rest or during sleep is common and if
tachycardia does not terminate it can lead to ventricular fibrillation and
death. A mutation in Glycerol-3-phosphate dehydrogenase 1-like gene (GPD1L), an
ion channel modulator in the heart, is linked to Brugada
Syndrome inherited as autosomal dominant and more common in Asian males. Co-expression
of A280V GPD1-L with SCN5A gene in HEK cells reduces inward Na+ currents ~50%
to induce Brugada syndrome. We used a structure-based
approach to identify a novel inhibitor anti-arrhythmic GPD1-L protein with
atomic coordinates of small molecules through PubChem. Molecular docking based
on Argus Lab combined with the large well-characterized database of small
molecules, allowed for rapid turnaround time for molecular docking for top
scoring compounds blocking GPD1-L protein. Propafenone
exhibited high binding affinity to PHE 93 with low energy of 8.82743 Kcal/mol but free -14.5097 kcal/mol.
Keywords: BrS, GPD1-L, ST segment, ion channel, ventricular
fibrillation, SCN5A, HEK cell.
FULL-TEXT (SUBSCRIBE OR
PURCHASE TITLE)