Synthesis of alpha amylase inhibitors based on privileged indole scaffold

Synthesis of alpha amylase inhibitors based on privileged indole scaffold

Twenty five derivatives of indole carbohydrazide (1–25) had been synthesized. These compounds were characterized using 1H NMR and EI-MS, and further evaluated for their α-amylase inhibitory potential. The analogs (1–25) showed varying degree of α-amylase inhibitory potential. ranging between 9.28 an...

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Published in:Bioorganic Chemistry
Main Author: Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
Format: Article
Language:English
Published: Academic Press Inc. 2017
Online Access:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85018732634&doi=10.1016%2fj.bioorg.2017.04.010&partnerID=40&md5=c1e0613a6e04e30e2cf7fbb9284b98e3
id 2-s2.0-85018732634
spelling 2-s2.0-85018732634
Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
Synthesis of alpha amylase inhibitors based on privileged indole scaffold
2017
Bioorganic Chemistry
72

10.1016/j.bioorg.2017.04.010
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85018732634&doi=10.1016%2fj.bioorg.2017.04.010&partnerID=40&md5=c1e0613a6e04e30e2cf7fbb9284b98e3
Twenty five derivatives of indole carbohydrazide (1–25) had been synthesized. These compounds were characterized using 1H NMR and EI-MS, and further evaluated for their α-amylase inhibitory potential. The analogs (1–25) showed varying degree of α-amylase inhibitory potential. ranging between 9.28 and 599.0 µM when compared with standard acarbose having IC50 value 8.78 ± 0.16 µM. Six analogs, 25 (IC50 = 9.28 ± 0.153 µM), 22 (IC50 = 9.79 ± 0.43 µM), 4 (IC50 = 11.08 ± 0.357 µM), 1 (IC50 = 12.65 ± 0.169 µM), 8 (IC50 = 21.37 ± 0.07 µM) and 14 (IC50 = 43.21 ± 0.14 µM) showed potent α-amylase inhibition as compared to the standard acarbose (IC50 = 8.78 ± 0.16 µM). All other analogs displayed good to moderate inhibitory potential. Structure-activity relationship was established through the interaction of the active compounds with enzyme active site with the help of docking studies. © 2017 Elsevier Inc.
Academic Press Inc.
452068
English
Article
author Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
spellingShingle Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
Synthesis of alpha amylase inhibitors based on privileged indole scaffold
author_facet Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
author_sort Noreen T.; Taha M.; Imran S.; Chigurupati S.; Rahim F.; Selvaraj M.; Ismail N.H.; Mohammad J.I.; Ullah H.; javid M.T.; Nawaz F.; Irshad M.; Ali M.
title Synthesis of alpha amylase inhibitors based on privileged indole scaffold
title_short Synthesis of alpha amylase inhibitors based on privileged indole scaffold
title_full Synthesis of alpha amylase inhibitors based on privileged indole scaffold
title_fullStr Synthesis of alpha amylase inhibitors based on privileged indole scaffold
title_full_unstemmed Synthesis of alpha amylase inhibitors based on privileged indole scaffold
title_sort Synthesis of alpha amylase inhibitors based on privileged indole scaffold
publishDate 2017
container_title Bioorganic Chemistry
container_volume 72
container_issue
doi_str_mv 10.1016/j.bioorg.2017.04.010
url https://www.scopus.com/inward/record.uri?eid=2-s2.0-85018732634&doi=10.1016%2fj.bioorg.2017.04.010&partnerID=40&md5=c1e0613a6e04e30e2cf7fbb9284b98e3
description Twenty five derivatives of indole carbohydrazide (1–25) had been synthesized. These compounds were characterized using 1H NMR and EI-MS, and further evaluated for their α-amylase inhibitory potential. The analogs (1–25) showed varying degree of α-amylase inhibitory potential. ranging between 9.28 and 599.0 µM when compared with standard acarbose having IC50 value 8.78 ± 0.16 µM. Six analogs, 25 (IC50 = 9.28 ± 0.153 µM), 22 (IC50 = 9.79 ± 0.43 µM), 4 (IC50 = 11.08 ± 0.357 µM), 1 (IC50 = 12.65 ± 0.169 µM), 8 (IC50 = 21.37 ± 0.07 µM) and 14 (IC50 = 43.21 ± 0.14 µM) showed potent α-amylase inhibition as compared to the standard acarbose (IC50 = 8.78 ± 0.16 µM). All other analogs displayed good to moderate inhibitory potential. Structure-activity relationship was established through the interaction of the active compounds with enzyme active site with the help of docking studies. © 2017 Elsevier Inc.
publisher Academic Press Inc.
issn 452068
language English
format Article
accesstype
record_format scopus
collection Scopus
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