©1996-2017. 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 18(1):30-38, 2017
In silico docking
of hydrazone derivatives with Sortase A from Staphylococcus aureus.
V
Laxmi Prasanna1, R Narender.2
1Asst. Prof Chemistry Vignan institute of
technology and science Deshmukhi, 2Professor Chemistry, CMR College of Engineering & Technology, Kandlakoya, Hyderabad, India.
ABSTRACT
Prasanna VL, Narender R., In
silico docking hydrazone derivative with Sortase A from Staphylococcus aureus, Onl
J Bioinform., 18(1):30-38, 2017. Sortase A (from Staphylococcus aureus) model
was built by homology-modeling with the MODELLER program. The 3-D structure of Sortase A from Staphylococcus aureus was used as a target
to determine binding, inhibitor binding position and affinities using GOLD
software scoring fitness functions. Structures of synthesized compounds were
confirmed by 1H NMR and Mass spectral data. Synthesized hydrazone
derivative 4a-4g was a mixture
of rotameric antiperiplanar
and synperiplanar spectra. In
silico binding to
bacterial protein confirmed inhibitory activity. Amino acid residues ARG130, ASP132,
SER133, VAL 134, ASP135, PHE136, GLN152 in Sortase A were involved in
inhibitor recognition via hydrogen bonding interactions which stabilized target-ligand complex. The results suggest that conserved amino-acid residues in Sortase A may affect functional conformation and are directly involved in
donor substrate binding.
Key words: Docking, insilico studies,
Sortase A, Staphylococcus aureus.