Rapid analysis of chemical composition in the active extract against α-amylase from blaps rynchopetera fairmaire by GC-MS and in silico theoretical explanation

References

• Zhang, L. S.; Xia, C. L.; Yang, Y. S.; Liu, G. M. Progress on Studies of Blaps Rynchopetera Fairmaire of the Yi Nationality. Lishizhen Med. Mater. Med. Res. 2009, 20, 3113–3114.
   Google Scholar
• Xiao, H.; Dong, J. W.; Zhou, D. J.; Wu, X. M.; Luo, J. R.; Zhang, C. G.; Guo, N. N.; Li, Y.; Cai, L.; Ding, Z. T. Cytotoxicity of the Defensive Secretion from the Medicinal Insect Blaps Rynchopetera. Molecules 2017, 23, 10.
   Web of Science ®Google Scholar
• Luo, Q.; Cai, L.; Wu, X. M.; Guo, N. N.; Luo, J. R.; H, X. Cyclodipeptides from Medicinal Insect Blaps Rynchopetera. Chin. Tradit. Herb. Drugs 2015, 46, 2381–2384.
   Google Scholar
• Xiao, H.; Yin, T. P.; Dong, J. W.; Wu, X. M.; Luo, Q.; Luo, J. R.; Cai, L.; Ding, Z. T. Five New Phenolic Compounds with Antioxidant Activities from the Medicinal Insect Blaps Rynchopetera. Molecules 2017, 22, 1301. DOI: 10.3390/molecules22081301.
   Web of Science ®Google Scholar
• Ali, H.; Houghton, P. J.; Soumyanath, A. alpha-Amylase Inhibitory Activity of Some Malaysian Plants Used to Treat Diabetes with Particular Reference to Phyllanthus Amarus. J. Ethnopharmacol. 2006, 107, 449–455.
   PubMed Web of Science ®Google Scholar
• Picot, M. C. N.; Zengin, G.; Mollica, A.; Stefanucci, A.; Carradori, S.; Mahomoodally, M. F. In Vitro and in Silico Studies of Mangiferin from Aphloia Theiformis on Key Enzymes Linked to Diabetes Type 2 and Associated Complications. Med. Chem. 2017, 13, 633–640.
   PubMed Web of Science ®Google Scholar
• Stefanucci, A.; Marrone, A.; Agamennone, M. Investigation of the N-BP Binding at FPPS by Combined Computational Approaches. Med. Chem. 2015, 11, 417–431.
   PubMed Web of Science ®Google Scholar
• Mollica, A.; Mirzaie, S.; Costante, R.; Carradori, S.; Macedonio, G.; Stefanucci, A.; Dvoracsko, S.; Novellino, E. Exploring the Biological Consequences of Conformational Changes in Aspartame Models Containing Constrained Analogues of Phenylalanine. J. Enzyme Inhib. Med. Chem. 2016, 31, 953–963. DOI: 10.3109/14756366.2015.1076811.
   PubMed Web of Science ®Google Scholar
• Wang, X.; Liu, Y.; Wang, H. A Structure-Differential Binding Method for Elucidating the Interactions between Flavonoids and Cytochrome-c by ESI-MS and Molecular Docking. Talanta 2013, 116, 368–375. DOI: 10.1016/j.talanta.2013.05.061.
   PubMed Web of Science ®Google Scholar
• Walker, S. D.; McEldowney, S. Molecular Docking: A Potential Tool to Aid Ecotoxicity Testing in Environmental Risk Assessment of Pharmaceuticals. Chemosphere 2013, 93, 2568–2577. DOI: 10.1016/j.chemosphere.2013.09.074.
   PubMed Web of Science ®Google Scholar
• Guo, X.; Gu, D.; Wang, M.; Huang, Y.; Li, H.; Dong, Y.; Tian, J.; Wang, Y.; Yang, Y. Characterization of Active Compounds from Gracilaria Lemaneiformis Inhibiting the Protein Tyrosine Phosphatase 1B Activity. Food Funct. 2017, 8, 3271–3275. DOI: 10.1039/C7FO00376E.
   PubMed Web of Science ®Google Scholar
• Tan, Y.; Chang, S. K. C.; Zhang, Y. Comparison of α-Amylase, α-Glucosidase and Lipase Inhibitory Activity of the Phenolic Substances in Two Black Legumes of Different Genera. Food Chem. 2017, 214, 259–268. DOI: 10.1016/j.foodchem.2016.06.100.
   PubMed Web of Science ®Google Scholar
• Adisakwattana, S.; Lerdsuwankij, O.; Poputtachai, U.; Minipun, A.; Suparpprom, C. Inhibitory Activity of Cinnamon Bark Species and Their Combination Effect with Acarbose against Intestinal α-Glucosidase and Pancreatic α-Amylase. Plant Foods Hum. Nutr. 2011, 66, 143–148. DOI: 10.1007/s11130-011-0226-4.
   PubMed Web of Science ®Google Scholar
• Chandra; Puttaraju, K. B.; Mahesh, S. S.; Shivashankar, K.; Lokanath, N. K.; Madegowda, M. Molecular Docking Studies of Benzimidazopyri Midine and Coumarin Substituted Benzimidazopyrimidine Derivatives: As Potential Human Aurora a Kinase Inhibitors. Bioinformation 2014, 10, 288–292.
   PubMedGoogle Scholar
• Berman, H. M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T. N.; Weissig, H.; Shindyalov, I. N.; Bourne, P. E. The Protein Data Bank. Nucleic Acids Res. 2000, 28, 235–242. DOI: 10.1093/nar/28.1.235.
   PubMed Web of Science ®Google Scholar
• Brayer, G. D.; Luo, Y.; Withers, S. G. The Structure of Human Pancreatic Alpha-Amylase at 1.8 A Resolution and Comparisons with Related Enzymes. Protein Sci. 1995, 4, 1730–1742. DOI: 10.1002/pro.5560040908.
   PubMed Web of Science ®Google Scholar
• Gogoi, P.; Kanaujia, S. P. Role of Structural Features in Oligomerization, Active-Site Integrity and Ligand Binding of Ribose-1,5-Bisphosphate Isomerase. Comput. Struct. Biotechnol. J 2019, 17, 333–344. DOI: 10.1016/j.csbj.2019.02.009.
   PubMedGoogle Scholar
• Mollica, A.; Stefanucci, A.; Zengin, G.; Locatelli, M.; Macedonio, G.; Orlando, G.; Ferrante, C.; Menghini, L.; Recinella, L.; Leone, S.; et al. Polyphenolic Composition, Enzyme Inhibitory Effects Ex-Vivo and in-Vivo Studies on Two Brassicaceae of North-Central Italy. Biomed. Pharmacother. 2018, 107, 129–138. DOI: 10.1016/j.biopha.2018.07.169.
   PubMed Web of Science ®Google Scholar
• Mahomoodally, M. F.; Mollica, A.; Stefanucci, A.; Aumeeruddy, M. Z.; Poorneeka, R.; Zengin, G. Volatile Components, Pharmacological Profile, and Computational Studies of Essential Oil from Aegle Marmelos (Bael) Leaves: A Functional Approach. Ind. Crops Prod. 2018, 126, 13–21. DOI: 10.1016/j.indcrop.2018.09.054.
   Web of Science ®Google Scholar
• Zengin, G.; Locatelli, M.; Stefanucci, A.; Macedonio, G.; Novellino, E.; Mirzaie, S.; Dvorácskó, S.; Carradori, S.; Brunetti, L.; Orlando, G.; et al. Chemical Characterization, Antioxidant Properties, Anti-Inflammatory Activity, and Enzyme Inhibition of Ipomoea batatas L. Leaf Extracts. Int. J. Food Prop. 2017, 20, 1907–1919. DOI: 10.1080/10942912.2017.1357127.
   Web of Science ®Google Scholar
• Zengin, G.; Rodrigues, M. J.; Abdallah, H. H.; Custodio, L.; Stefanucci, A.; Aumeeruddy, mz.; Mollica, A.; Rengasamy, K. R.; Mahomoodally, M. F. Combination of Phenolic Profiles, Pharmacological Properties and in Silico Studies to Provide New Insights on Silene Salsuginea from Turkey. Comput. Biol. Chem. 2018, 77, 178–186. DOI: 10.1016/j.compbiolchem.2018.10.005.
   PubMed Web of Science ®Google Scholar
• Li, L.; Wei, S.; Zhu, T.; Xue, G.; Xu, D.; Wang, W.; Wang, X.; Luo, J.; Kong, L. Anti-Inflammatory Norabietane Diterpenoids from the Leaves of Salvia Officinalis L. J. Funct. Foods 2019, 54, 154–163. DOI: 10.1016/j.jff.2019.01.020.
   Web of Science ®Google Scholar
• Luo, J.; Zhang, Z.; Yang, Y.; Liu, G. Analysis of the Fat-Soluble Components in Blaps Rynchopetera Fairmaire by GC-MS. Lishizhen Med. Mater. Med. Res. 2010, 21, 12–13.
   Google Scholar
• Xu, F.; Gu, D.; Wang, M.; Zhu, L.; Chu, T.; Cui, Y.; Tian, J.; Wang, Y.; Yang, Y. Screening of the Potential α-Amylase Inhibitor in Essential Oil from Cedrus Deodara Cones. Ind. Crops Prod. 2017, 103, 251–256. DOI: 10.1016/j.indcrop.2017.04.006.
   Web of Science ®Google Scholar
• Gu, D.; Fang, C.; Yang, J.; Li, M.; Liu, H.; Yang, Y. Chemical Composition and α-Amylase Inhibitory Activity of the Essential Oil from Sabina Chinensis cv. Kaizuca Leaves. Nat. Prod. Res. 2018, 32, 711–713. DOI: 10.1080/14786419.2017.1332612.
   PubMed Web of Science ®Google Scholar
• Yang, J.; Gu, D.; Wang, M.; Kou, D.; Guo, H.; Tian, J.; Yang, Y. In Silico-Assisted Identification of α-Amylase Inhibitor from the Needle Oil of Pinus Tabulaeformis Carr. Ind. Crops Prod. 2018, 111, 360–363.
   Web of Science ®Google Scholar
• Sharifi, N.; Souri, E.; Ziai, S. A.; Amin, G.; Amini, M.; Amanlou, M. Isolation, Identification and Molecular Docking Studies of a New Isolated Compound, from Onopordon Acanthium: A Novel Angiotensin Converting Enzyme (ACE) Inhibitor. J. Ethnopharmacol. 2013, 148, 934–939. DOI: 10.1016/j.jep.2013.05.046.
   PubMed Web of Science ®Google Scholar
• Kratz, M.; Marcovina, S.; Nelson, J. E.; Yeh, M. M.; Kowdley, K. V.; Callahan, H. S.; Song, X.; Di, C.; Utzschneider, K. M. Dairy Fat Intake Is Associated with Glucose Tolerance, Hepatic and Systemic Insulin Sensitivity, and Liver Fat but Not β-Cell Function in Humans. Am. J. Clin. Nutr. 2014, 99, 1385–1396. DOI: 10.3945/ajcn.113.075457.
   PubMed Web of Science ®Google Scholar
• Santaren, I. D.; Watkins, S. M.; Liese, A. D.; Wagenknecht, L. E.; Rewers, M. J.; Haffner, S. M.; Lorenzo, C.; Hanley, A. J. Serum Pentadecanoic Acid (15:0), a Short-Term Marker of Dairy Food Intake, Is Inversely Associated with Incident Type 2 Diabetes and Its Underlying Disorders. Am. J. Clin. Nutr. 2014, 100, 1532–1540. DOI: 10.3945/ajcn.114.092544.
   PubMed Web of Science ®Google Scholar
• Jenkins, B.; West, J. A.; Koulman, A. A Review of Odd-Chain Fatty Acid Metabolism and the Role of Pentadecanoic Acid (C15:0) and Heptadecanoic Acid (C17:0) in Health and Disease. Molecules 2015, 20, 2425–2444. DOI: 10.3390/molecules20022425.
   PubMed Web of Science ®Google Scholar
• Wang, H.; Gu, D.; Wang, M.; Guo, H.; Wu, H.; Tian, G.; Li, Q.; Yang, Y.; Tian, J. A Strategy Based on Gas Chromatography-Mass Spectrometry and Virtual Molecular Docking for Analysis and Prediction of Bioactive Composition in Natural Product Essential Oil. J. Chromatogr. A 2017, 1501, 128–133. DOI: 10.1016/j.chroma.2017.04.031.
   PubMed Web of Science ®Google Scholar
• Yang, Y.; Gu, D.; Yili, A.; Zhao, Y.; He, D.; Aisa, H. A. One-Step Separation and Purification of Rupestonic Acid and Chrysosptertin B from Artemisia Rupestris L. by High-Speed Counter-Current Chromatography. Phytochem. Anal. 2010, 21, 205–209.
   PubMed Web of Science ®Google Scholar