Evaluación in silico de la interacción de la enzima DPP-IV con derivados del ácido CAFEICO
DOI:
https://doi.org/10.61117/ipsumtec.v6i4.266Palabras clave:
Derivados del ácido cafeico, Inhibición enzimática, Ensayos in silico, Acoplamiento molecularResumen
Este estudio tuvo como objetivo evaluar mediante herramientas in silico el potencial inhibidor de la enzima Dipeptidil-peptidasa-4 (DPP-IV) de los derivados del ácido cafeico. El ácido cafeico es un compuesto orgánico clasificado como ácido hidroxicinámico, se puede encontrar en una variedad de bebidas, como café preparado, en frutas, hierbas y especias. En primer lugar, se predijo la biotransformación metabólica del ácido cafeico mediante el servidor web Way2Drug y, a continuación, se determinó el acoplamiento molecular mediante el programa AutoDock Vina. Los resultados mostraron que la O-glucuronidación y la O-sulfatación fueron las principales reacciones encontradas y pertenecen a la fase II del metabolismo. Según el análisis in silico, el ácido cafeico 3-O-glucurónido y el ácido cafeico 4-O-glucurónido fueron los principales derivados del ácido cafeico que exhibieron las energías libres de afinidad más altas con la enzima DPP-IV (-8.0 y -8.1 kcal/mol, respectivamente) en comparación con los metabolitos sulfatados. Este estudio allana el camino para identificar los metabolitos glucuronizados del ácido cafeico como inhibidores potenciales de la DPP-IV, una enzima con un papel importante en el metabolismo de la glucosa.
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Coll, C., Colomina, R., Onrubia, J. y Rochera, M. J. (1992). Actividad conjunta y habla: una aproximación al estudio de los mecanismos de influencia educativa. Infancia y Aprendizaje, 59-60, pp.189-232. DOI: https://doi.org/10.1080/02103702.1992.10822356
Singh AK, Yadav D, Sharma N, Jin JO (2021). Dipeptidyl Peptidase (DPP)-IV Inhibitors with Antioxidant Potential Isolated from Natural Sources: A Novel Approach for the Management of Diabetes. Pharmaceuticals 14:586. DOI: https://doi.org/10.3390/ph14060586
Gribble FM, Reimann F (2021). Metabolic Messengers: glucagon-like peptide 1. Nat Metab 3:142–148. DOI: https://doi.org/10.1038/s42255-020-00327-x
Fan J, Johnson MH, Lila MA, et al (2013). Berry and citrus phenolic compounds inhibit dipeptidyl peptidase IV: Implications in diabetes management. Evidence-based Complement Altern Med 2013. DOI: https://doi.org/10.1155/2013/479505
Di Stefano E, Tsopmo A, Oliviero T, et al (2019). Bioprocessing of common pulses changed seed microstructures, and improved dipeptidyl peptidase-IV and α-glucosidase inhibitory activities. Sci Rep 9:15308. DOI: https://doi.org/10.1038/s41598-019-51547-5
Dai L, Kong L, Cai X, et al (2022). Analysis of the Structure and Activity of Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Oligopeptides from Sorghum Kafirin. J Agric Food Chem 70:2010–2017. DOI: https://doi.org/10.1021/acs.jafc.1c04484
Cian RE, Albarracín M, Garzón AG, Drago SR (2022). Precooked sorghum flour as proper vehicle of ACE‐I and DPP‐IV inhibitory sorghum peptides. Int J Food Sci Technol 57:4832–4839. DOI: https://doi.org/10.1111/ijfs.15718
Xu F, Xu B, Chen H, et al (2022). Enhancement of DPP-IV inhibitory activity and the capacity for enabling GLP-1 secretion through RADA16-assisted molecular designed rapeseed peptide nanogels. Food Funct 13:5215–5228. DOI: https://doi.org/10.1039/D1FO04367F
El Gharras H (2009). Polyphenols: food sources, properties and applications - a review. Int J Food Sci Technol 44:2512–2518. DOI: https://doi.org/10.1111/j.1365-2621.2009.02077.x
Birková A (2020). Caffeic acid: a brief overview of its presence, metabolism, and bioactivity. Bioact Compd Heal Dis 3:74. DOI: https://doi.org/10.31989/bchd.v3i4.692
Ramírez K, Quintero-Soto MF, Rochín-Medina JJ (2020). Enhancement of the antioxidant and antimicrobial activities of maize wastewater by an eco-friendly process. J Food Meas Charact 14:1682–1689. DOI: https://doi.org/10.1007/s11694-020-00416-1
Rochín-Medina JJ, López-Moreno HS, Ramírez K (2021). Effect of Bacillus clausii-fermented spent coffee ground extract on Salmonella-infected macrophages. Lwt 137:. DOI: https://doi.org/10.1016/j.lwt.2020.110429
Istyastono EP, Octa Riswanto FD (2022). Molecular Dynamics Simulations of the Caffeic Acid Interactions to Dipeptidyl Peptidase IV. Int J Appl Pharm 14:274–278. DOI: https://doi.org/10.22159/ijap.2022v14i4.44631
Balogun FO, Naidoo K, Aribisala JO, et al (2022). Cheminformatics Identification and Validation of Dipeptidyl Peptidase-IV Modulators from Shikimate Pathway-Derived Phenolic Acids towards Interventive Type-2 Diabetes Therapy. Metabolites 12:937. DOI: https://doi.org/10.3390/metabo12100937
Truzzi F, Tibaldi C, Zhang Y, et al (2021). An Overview on Dietary Polyphenols and Their Biopharmaceutical Classification System (BCS). Int J Mol Sci 22:5514. DOI: https://doi.org/10.3390/ijms22115514
Sova M, Saso L (2020). Natural sources, pharmacokinetics, biological activities and health benefits of hydroxycinnamic acids and their metabolites. Nutrients 12:1–30. DOI: https://doi.org/10.3390/nu12082190
de Ruyck J, Brysbaert G, Blossey R, Lensink M (2016). Molecular docking as a popular tool in drug design, an in silico travel. Adv Appl Bioinforma Chem Volume 9:1–11. DOI: https://doi.org/10.2147/AABC.S105289
Tao X, Huang Y, Wang C, et al (2020). Recent developments in molecular docking technology applied in food science: a review. Int J Food Sci Technol 55:33–45. DOI: https://doi.org/10.1111/ijfs.14325
Rudik AV, Dmitriev AV, Lagunin AA, et al (2016). Prediction of reacting atoms for the major biotransformation reactions of organic xenobiotics. J Cheminform 8:68. DOI: https://doi.org/10.1186/s13321-016-0183-x
Reyes-Chaparro A, Verdín-Betancourt FA, Sierra-Santoyo A (2020). Human Biotransformation Pathway of Temephos Using an in silico Approach. Chem Res Toxicol 33:2765–2774. DOI: https://doi.org/10.1021/acs.chemrestox.0c00105
Namoto K, Sirockin F, Ostermann N, et al (2014). Discovery of C-(1-aryl-cyclohexyl)-methylamines as selective, orally available inhibitors of dipeptidyl peptidase IV. Bioorg Med Chem Lett 24:731–736. DOI: https://doi.org/10.1016/j.bmcl.2013.12.118
Choi WG, Kim JH, Kim D, et al (2018). Simultaneous Determination of Chlorogenic Acid Isomers and Metabolites in Rat Plasma Using LC-MS/MS and Its Application to A Pharmacokinetic Study Following Oral Administration of Stauntonia hexaphylla Leaf Extract (YRA-1909) to Rats. Pharmaceutics 10:143. DOI: https://doi.org/10.3390/pharmaceutics10030143
Stalmach A, Mullen W, Barron D, et al (2009). Metabolite Profiling of Hydroxycinnamate Derivatives in Plasma and Urine after the Ingestion of Coffee by Humans: Identification of Biomarkers of Coffee Consumption. Drug Metab Dispos 37:1749–1758. DOI: https://doi.org/10.1124/dmd.109.028019
Bjelke JR, Christensen J, Branner S, et al (2004). Tyrosine 547 Constitutes an Essential Part of the Catalytic Mechanism of Dipeptidyl Peptidase IV. J Biol Chem 279:34691–34697. DOI: https://doi.org/10.1074/jbc.M405400200
Kirby M, Yu DMT, O’Connor S, Gorrell MD (2010). Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition. Clin Sci 118:31–41. DOI: https://doi.org/10.1042/CS20090047
Abbott CA, McCaughan GW, Gorrell MD (1999). Two highly conserved glutamic acid residues in the predicted β-propeller domain of dipeptidyl peptidase IV are required for its enzyme activity. FEBS Lett 458:278–284. DOI: https://doi.org/10.1016/S0014-5793(99)01166-7
Ahren B (2010). Use of DPP-4 inhibitors in type 2 diabetes: focus on sitagliptin. Diabetes, Metab Syndr Obes Targets Ther 3:31–41. DOI: https://doi.org/10.2147/DMSO.S7327
Pan J, Zhang Q, Zhang C, et al (2022). Inhibition of Dipeptidyl Peptidase-4 by Flavonoids: Structure–Activity Relationship, Kinetics and Interaction Mechanism. Front Nutr 9:1–17. DOI: https://doi.org/10.3389/fnut.2022.892426
Tuersuntuoheti T, Pan F, Zhang M, et al (2022). Prediction of DPP‐IV Inhibitory Potentials of Polyphenols Existed in Qingke Barley Fresh Noodles: In Vitro and In Silico Analyses. J Food Process Preserv e16808. DOI: https://doi.org/10.1111/jfpp.16808
Li M, Bao X, Zhang X, et al (2022). Exploring the phytochemicals and inhibitory effects against α-glucosidase and dipeptidyl peptidase-IV in Chinese pickled chili pepper: Insights into mechanisms by molecular docking analysis. LWT 162:113467. DOI: https://doi.org/10.1016/j.lwt.2022.113467
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Derechos de autor 2023 Jesús Jaime Rochín-Medina, K. Ramírez, Ilianne A. Mendoza-López, Estephany Siomara Ramírez-Serrano
Esta obra está bajo una licencia internacional Creative Commons Atribución 4.0.
