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Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies

[Image: see text] Diabetes mellitus (DM) is a complex and multiple group of disorders, and understanding the molecular mechanisms is a key role in identifying various markers involved in the diagnosis of the disease. Brucine is derived from the seeds of Strychnos nux-vomica L. (Loganiaceae), which h...

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Autores principales: Khan, Naimat Ullah, Qazi, Neelum Gul, Khan, Arif-ullah, Ali, Fawad, Hassan, Syed Shams ul, Bungau, Simona
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9774404/
https://www.ncbi.nlm.nih.gov/pubmed/36570195
http://dx.doi.org/10.1021/acsomega.2c04977
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author Khan, Naimat Ullah
Qazi, Neelum Gul
Khan, Arif-ullah
Ali, Fawad
Hassan, Syed Shams ul
Bungau, Simona
author_facet Khan, Naimat Ullah
Qazi, Neelum Gul
Khan, Arif-ullah
Ali, Fawad
Hassan, Syed Shams ul
Bungau, Simona
author_sort Khan, Naimat Ullah
collection PubMed
description [Image: see text] Diabetes mellitus (DM) is a complex and multiple group of disorders, and understanding the molecular mechanisms is a key role in identifying various markers involved in the diagnosis of the disease. Brucine is derived from the seeds of Strychnos nux-vomica L. (Loganiaceae), which has been used in traditional medicine to cure a variety of ailments, such as chronic rheumatism, nervous system diseases, dyspepsia, gonorrhea, anemia, and bronchitis, and has analgesic, anti-inflammatory, anti-oxidant, anti-snake venom, and anti-diabetic properties. The anti-diabetic potential of brucine was studied utilizing in vitro, in silico, in vivo, and molecular methods, including streptozotocin-induced diabetic rat models, α-glucosidase and α-amylase inhibitory assays, and via Auto-DocVina software. Brucine exhibits binding affinities of −5.0 to −10.1 Kcal/mol against chosen protein targets, according to an in silico investigation. In vitro studies revealed that brucine inhibited the enzymes α-amylase and α-glucosidase, and brucine (20 mg/kg) reduced blood glucose levels, oral glucose tolerance overload, body weight, glycosylated hemoglobin levels, total cholesterol, triglycerides, low-density lipoprotein, alanine transaminase, aspartate aminotransferase, total bilirubin, and alkaline phosphatase and elevated high-density lipoprotein levels in in vivo studies. The brucine binding energy against certain protein targets ranges from −5.0 to −10.1 Kcal/mol. It has anti-diabetic, anti-hyperlipidemic, hepatoprotective, anti-oxidant, and anti-inflammatory properties, which are mediated via inhibition of α-glucosidase and α-amylase.
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spelling pubmed-97744042022-12-23 Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies Khan, Naimat Ullah Qazi, Neelum Gul Khan, Arif-ullah Ali, Fawad Hassan, Syed Shams ul Bungau, Simona ACS Omega [Image: see text] Diabetes mellitus (DM) is a complex and multiple group of disorders, and understanding the molecular mechanisms is a key role in identifying various markers involved in the diagnosis of the disease. Brucine is derived from the seeds of Strychnos nux-vomica L. (Loganiaceae), which has been used in traditional medicine to cure a variety of ailments, such as chronic rheumatism, nervous system diseases, dyspepsia, gonorrhea, anemia, and bronchitis, and has analgesic, anti-inflammatory, anti-oxidant, anti-snake venom, and anti-diabetic properties. The anti-diabetic potential of brucine was studied utilizing in vitro, in silico, in vivo, and molecular methods, including streptozotocin-induced diabetic rat models, α-glucosidase and α-amylase inhibitory assays, and via Auto-DocVina software. Brucine exhibits binding affinities of −5.0 to −10.1 Kcal/mol against chosen protein targets, according to an in silico investigation. In vitro studies revealed that brucine inhibited the enzymes α-amylase and α-glucosidase, and brucine (20 mg/kg) reduced blood glucose levels, oral glucose tolerance overload, body weight, glycosylated hemoglobin levels, total cholesterol, triglycerides, low-density lipoprotein, alanine transaminase, aspartate aminotransferase, total bilirubin, and alkaline phosphatase and elevated high-density lipoprotein levels in in vivo studies. The brucine binding energy against certain protein targets ranges from −5.0 to −10.1 Kcal/mol. It has anti-diabetic, anti-hyperlipidemic, hepatoprotective, anti-oxidant, and anti-inflammatory properties, which are mediated via inhibition of α-glucosidase and α-amylase. American Chemical Society 2022-12-08 /pmc/articles/PMC9774404/ /pubmed/36570195 http://dx.doi.org/10.1021/acsomega.2c04977 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Khan, Naimat Ullah
Qazi, Neelum Gul
Khan, Arif-ullah
Ali, Fawad
Hassan, Syed Shams ul
Bungau, Simona
Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies
title Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies
title_full Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies
title_fullStr Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies
title_full_unstemmed Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies
title_short Anti-diabetic Activity of Brucine in Streptozotocin-Induced Rats: In Silico, In Vitro, and In Vivo Studies
title_sort anti-diabetic activity of brucine in streptozotocin-induced rats: in silico, in vitro, and in vivo studies
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9774404/
https://www.ncbi.nlm.nih.gov/pubmed/36570195
http://dx.doi.org/10.1021/acsomega.2c04977
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