{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T05:02:13Z","timestamp":1789707733828,"version":"4.0.1"},"reference-count":61,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T00:00:00Z","timestamp":1789516800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Key Research and Development Program of China","award":["2021YFD2100402"],"award-info":[{"award-number":["2021YFD2100402"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Foods"],"abstract":"<jats:p>This study systematically explored the inhibitory mechanisms against sucrase exerted by sugarcane molasses polyphenol extract (SMPE) and its three principal chlorogenic acid analogs: neochlorogenic acid (NA), chlorogenic acid (CA), and methyl chlorogenate (MC). By integrating in vitro assays, molecular simulations, and spectroscopic analyses, we demonstrated synergistic inhibition among the components. SMPE exhibited the greatest inhibitory potency (IC50 = 3.58 \u00b1 0.16 mg\/mL), with an IC50 significantly lower than those of the individual compounds. Synergy analysis indicated marked synergistic effects for both the CA-NA pair and the ternary mixture. Simultaneous multi-ligand docking further suggested complementary co-binding configurations and interactions with residues surrounding the catalytic region, providing a possible structural interpretation of the experimentally observed synergistic effects. Mechanistically, CA and NA exhibited competitive inhibition, whereas MC and SMPE showed mixed-type inhibition; fluorescence, CD, and thermal stability analyses revealed compound-dependent changes in aromatic residue microenvironments, secondary structure, and protein stability, while molecular modeling predicted peripheral binding of CA\/NA and catalytic-region interactions of MC, suggesting distinct but complementary routes for perturbing substrate recognition and catalysis. This study provides mechanistic insight into the synergistic inhibition of sucrase by SMPE and supports its potential development as a natural agent for modulating postprandial glycemia.<\/jats:p>","DOI":"10.3390\/foods15183267","type":"journal-article","created":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T07:58:59Z","timestamp":1789545539000},"page":"3267","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Synergistic Orchestration of Chlorogenic Acid Analogs in Sugarcane Molasses Polyphenols for Sucrase Inhibition: Insights into a Multilevel Inhibitory Mechanism"],"prefix":"10.3390","volume":"15","author":[{"given":"Shenghong","family":"Yao","sequence":"first","affiliation":[{"name":"Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-original-draft","vocabulary":"credit"}]},{"given":"Wanlu","family":"Liu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yumei","family":"Wang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-3215-1871","authenticated-orcid":false,"given":"Jiulong","family":"An","sequence":"additional","affiliation":[{"name":"Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Chengfeng","family":"Zhang","sequence":"additional","affiliation":[{"name":"The Product Makers Co., Ltd., Shanghai 200444, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7455-5162","authenticated-orcid":false,"given":"Matthew","family":"Flavel","sequence":"additional","affiliation":[{"name":"School of Life Sciences, La Trobe University, Melbourne 3083, Australia"},{"name":"The Product Makers (Australia), Keysborough 3173, Australia"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"given":"Yanv","family":"Zhou","sequence":"additional","affiliation":[{"name":"The Product Makers Co., Ltd., Shanghai 200444, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2299-6588","authenticated-orcid":false,"given":"Lu","family":"Li","sequence":"additional","affiliation":[{"name":"Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7459-9202","authenticated-orcid":false,"given":"He","family":"Li","sequence":"additional","affiliation":[{"name":"Key Laboratory of Geriatric Nutrition and Health, Beijing Technology and Business University, Ministry of Education, Beijing 100048, China"}],"role":[{"vocabulary":"crossref","role":"author"},{"role":"writing-original-draft","vocabulary":"credit"},{"role":"supervision","vocabulary":"credit"},{"role":"funding-acquisition","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"4562","DOI":"10.1039\/D5FO00090D","article-title":"Hypoglycemic potential of sugarcane molasses-derived polyphenols: Exploring the hypoglycemic mechanisms through in vitro alpha-glucosidase inhibition and intracellular glucose transport inhibition","volume":"16","author":"Zhao","year":"2025","journal-title":"Food Funct."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"4799","DOI":"10.1007\/s00018-020-03564-1","article-title":"A comprehensive overview of substrate specificity of glycoside hydrolases and transporters in the small intestine: \u201cA gut feeling\u201d","volume":"77","author":"Elferink","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"357","DOI":"10.2147\/DMSO.S28340","article-title":"Critical evaluation of the role of acarbose in the treatment of diabetes: Patient considerations","volume":"5","author":"Rosak","year":"2012","journal-title":"Diabetes Metab. Syndr. Obes."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"e115","DOI":"10.1002\/efd2.115","article-title":"Pomegranate peel polyphenols as an antioxidant additive for the development and characterization of a new active pectin edible film","volume":"4","author":"Aguilar","year":"2023","journal-title":"eFood"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1002\/anie.201000044","article-title":"Plant polyphenols: Chemical properties, biological activities, and synthesis","volume":"50","author":"Quideau","year":"2011","journal-title":"Angew. Chem.-Int. Edit."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"e88","DOI":"10.1002\/efd2.88","article-title":"Polyphenols in food Industry, nano-based technology development and biological properties: An overview","volume":"4","author":"Omidfar","year":"2023","journal-title":"eFood"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"141607","DOI":"10.1016\/j.molstruc.2025.141607","article-title":"Inhibitory mechanism of chlorogenic acid on \u03b1-glucosidase and evaluation of its glucose consumption in hepG2 cells","volume":"1331","author":"Jiang","year":"2025","journal-title":"J. Mol. Struct."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"130047","DOI":"10.1016\/j.foodchem.2021.130047","article-title":"Inhibition of \u03b1-glucosidases by tea polyphenols in rat intestinal extract and caco-2 Cells grown on transwell","volume":"361","author":"Kan","year":"2021","journal-title":"Food Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"114214","DOI":"10.1016\/j.indcrop.2021.114214","article-title":"Profiling of polyphenols by LC-QTOF\/ESI-MS, characteristics of nutritional compounds and in vitro effect on pancreatic lipase, \u03b1-glucosidase, \u03b1-amylase, cholinesterase and cyclooxygenase activities of sweet (Prunus avium) and sour (P. cerasus) cherries leaves and fruits","volume":"174","author":"Nowicka","year":"2021","journal-title":"Ind. Crop. Prod."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"4524","DOI":"10.1002\/jsfa.14187","article-title":"Inhibitory effects of phenolic compounds from blueberry leaf on \u03b1-amylase and \u03b1-glucosidase: Kinetics, mode of action, and molecular interactions","volume":"105","author":"Wu","year":"2025","journal-title":"J. Sci. Food Agric."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/s41664-024-00305-2","article-title":"Screening for bioactive compounds from mulberry leaves combining bio-affinity ultrafiltration with \u03b1-glucosidase and pancreatic lipase","volume":"8","author":"Zhang","year":"2024","journal-title":"J. Anal. Test."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Wang, Y., An, J., Yao, S., Zhang, C., Zhou, Y., Li, L., and Li, H. (2025). Effect of sugarcane polyphenol extract on \u03b1-amylase inhibition and mechanism exploration. Foods, 14.","DOI":"10.2139\/ssrn.5186044"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"126180","DOI":"10.1016\/j.foodchem.2020.126180","article-title":"Antioxidant activity and polyphenol composition of sugarcane molasses extract","volume":"314","author":"Deseo","year":"2020","journal-title":"Food Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"e13307","DOI":"10.1111\/1541-4337.13307","article-title":"Flavonoids and phenolic acids from sugarcane: Distribution in the plant, changes during processing, and potential benefits to industry and health","volume":"23","author":"Hewawansa","year":"2024","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"105775","DOI":"10.1016\/j.fbio.2024.105775","article-title":"Protective effects of polyphenol-rich sugarcane molasses extract against AGEs-induced glycosylation damage in L929 cells","volume":"63","author":"Wang","year":"2025","journal-title":"Food Biosci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"7270","DOI":"10.1021\/jf060808o","article-title":"Comparison of the concentrations of phenolic constituents in cane sugar manufacturing products with their antioxidant activities","volume":"54","author":"Payet","year":"2006","journal-title":"J. Agric. Food Chem."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Hewawansa, U.H.A.J., Barber, E., Houghton, M.J., Visvanathan, R., Nicolotti, L., Costa, R.J.S., and Williamson, G. (2026). Impact of acute (poly)phenol-rich sugarcane extract consumption on postprandial glycemic response in healthy adults: A randomized crossover study. Foods, 15.","DOI":"10.3390\/foods15040631"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1080\/07315724.2019.1587323","article-title":"Antioxidant and anti-diabetic functions of a polyphenol-rich sugarcane extract","volume":"38","author":"Ji","year":"2019","journal-title":"J. Am. Coll. Nutr."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/S0308-8146(02)00423-5","article-title":"Antioxidant capacity of phenolic phytochemicals from various cultivars of plums","volume":"81","author":"Kim","year":"2003","journal-title":"Food Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"7245","DOI":"10.1021\/jf3009958","article-title":"In vitro inhibitory effect on pancreatic lipase activity of subfractions from ethanol extracts of fermented oats (Avena sativa L.) and synergistic effect of three phenolic acids","volume":"60","author":"Cai","year":"2012","journal-title":"J. Agric. Food Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1021\/ja01318a036","article-title":"The determination of enzyme dissociation constants","volume":"56","author":"Lineweaver","year":"1934","journal-title":"J. Am. Chem. Soc."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"137749","DOI":"10.1016\/j.foodchem.2023.137749","article-title":"The inhibition mechanism of bound polyphenols extracted from mung bean coat dietary fiber on porcine pancreatic \u03b1-amylase: Kinetic, spectroscopic, differential scanning calorimetric and molecular docking","volume":"436","author":"Sun","year":"2024","journal-title":"Food Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.bpc.2006.07.006","article-title":"Sensitivity of p-glycoprotein tryptophan residues to benzodiazepines and ATP interaction","volume":"125","author":"Lima","year":"2007","journal-title":"Biophys. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"134434","DOI":"10.1016\/j.foodchem.2022.134434","article-title":"Identification of a novel \u03b1-amylase inhibitory activity peptide from quinoa protein hydrolysate","volume":"403","author":"Zhou","year":"2023","journal-title":"Food Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/bs.mie.2020.05.004","article-title":"Exploration of enzyme diversity: High-throughput techniques for protein production and microscale biochemical characterization","volume":"Volume 643","author":"Vasina","year":"2020","journal-title":"Methods in Enzymology"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Malm, L., Palm, E., Souihi, A., Plassmann, M., Liigand, J., and Kruve, A. (2021). Guide to semi-quantitative non-targeted screening using LC\/ESI\/HRMS. Molecules, 26.","DOI":"10.3390\/molecules26123524"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"109288","DOI":"10.1016\/j.lwt.2020.109288","article-title":"Inhibition of pancreatic \u03b1-amylase by lonicera caerulea berry polyphenols in vitro and their potential as hyperglycemic agents","volume":"126","author":"Liu","year":"2020","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1016\/j.foodchem.2017.11.027","article-title":"Inhibitory effects of edible seaweeds, polyphenolics and alginates on the activities of porcine pancreatic \u03b1-amylase","volume":"245","author":"Zaharudin","year":"2018","journal-title":"Food Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"3555","DOI":"10.1021\/jm800115x","article-title":"Flavonoids for controlling starch digestion: Structural requirements for inhibiting human \u03b1-amylase","volume":"51","author":"Scheib","year":"2008","journal-title":"J. Med. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1080\/10408398.2018.1548428","article-title":"The inhibitory effects of flavonoids on \u03b1-amylase and \u03b1-glucosidase","volume":"60","author":"Zhu","year":"2020","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1021\/acs.jcim.8b00266","article-title":"Salt bridge in ligand\u2013protein complexes\u2014Systematic theoretical and statistical investigations","volume":"58","author":"Kurczab","year":"2018","journal-title":"J. Chem. Inf. Model."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Xie, N., Du, Q., Li, J., and Huang, R. (2015). Exploring strong interactions in proteins with quantum chemistry and examples of their applications in drug design. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0137113"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"9755","DOI":"10.1074\/jbc.M112.446435","article-title":"Three-dimensional structure of saccharomyces invertase: Role of a non-catalytic domain in oligomerization and substrate specificity","volume":"288","author":"Lafraya","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.1039\/C7FO00236J","article-title":"An inhibition mechanism of dihydromyricetin on tyrosinase and the joint effects of vitamins B(6), D(3) or E","volume":"8","author":"Fan","year":"2017","journal-title":"Food Funct."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.jtbi.2014.04.032","article-title":"The additive damage model: A mathematical model for cellular responses to drug combinations","volume":"357","author":"Jones","year":"2014","journal-title":"J. Theor. Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1158\/0008-5472.CAN-09-1947","article-title":"Drug combination studies and their synergy quantification using the Chou-Talalay method","volume":"70","author":"Chou","year":"2010","journal-title":"Cancer Res."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Ramsay, R.R., and Tipton, K.F. (2017). Assessment of enzyme inhibition: A review with examples from the development of monoamine oxidase and cholinesterase inhibitory drugs. Molecules, 22.","DOI":"10.20944\/preprints201707.0019.v1"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"126750","DOI":"10.1016\/j.foodchem.2020.126750","article-title":"The binding mechanism between cyclodextrins and pullulanase: A molecular docking, isothermal titration calorimetry, circular dichroism and fluorescence study","volume":"321","author":"Li","year":"2020","journal-title":"Food Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1080\/14756366.2022.2076089","article-title":"Models of enzyme inhibition and apparent dissociation constants from kinetic analysis to study the differential inhibition of aldose reductase","volume":"37","author":"Balestri","year":"2022","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.foodchem.2016.03.093","article-title":"Interactions between polyphenols in thinned young apples and porcine pancreatic \u03b1-amylase: Inhibition, detailed kinetics and fluorescence quenching","volume":"208","author":"Sun","year":"2016","journal-title":"Food Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"111497","DOI":"10.1016\/j.foodres.2022.111497","article-title":"The inhibition mechanism of polyphenols from Phyllanthus Emblica Linn. fruit on acetylcholinesterase: A Interaction, kinetic, spectroscopic, and molecular simulation study","volume":"158","author":"Wu","year":"2022","journal-title":"Food Res. Int."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.tifs.2019.07.009","article-title":"Natural products for glycaemic control: Polyphenols as inhibitors of alpha-amylase","volume":"91","author":"Sun","year":"2019","journal-title":"Trends Food Sci. Technol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"127528","DOI":"10.1016\/j.foodchem.2020.127528","article-title":"The mechanism of chlorogenic acid inhibits lipid oxidation: An investigation using multi-spectroscopic methods and molecular docking","volume":"333","author":"Cao","year":"2020","journal-title":"Food Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1700324","DOI":"10.1002\/mnfr.201700324","article-title":"The mechanism of interactions between tea polyphenols and porcine pancreatic alpha-amylase: Analysis by inhibition kinetics, fluorescence quenching, differential scanning calorimetry and isothermal titration calorimetry","volume":"61","author":"Sun","year":"2017","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"11901","DOI":"10.1021\/jf103026x","article-title":"Study of the interaction of pancreatic lipase with procyanidins by optical and enzymatic methods","volume":"58","author":"Mateus","year":"2010","journal-title":"J. Agric. Food Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.saa.2018.05.011","article-title":"Comparing the binding interaction between \u03b2-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking","volume":"201","author":"Li","year":"2018","journal-title":"Spectrochim. Acta Part A Mol. Biomol. Spectrosc."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"129934","DOI":"10.1016\/j.foodchem.2021.129934","article-title":"Inhibition mechanism of diacylated anthocyanins from purple sweet potato (Ipomoea batatas L.) against \u03b1-amylase and \u03b1-glucosidase","volume":"359","author":"Yang","year":"2021","journal-title":"Food Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"109227","DOI":"10.1016\/j.foodhyd.2023.109227","article-title":"Mechanism of interaction between astaxanthin and soy protein fibrils: Effects on complexes structure, rheological properties and bioaccessibility","volume":"146","author":"Li","year":"2024","journal-title":"Food Hydrocoll."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Li, M., Ritzoulis, C., Du, Q., Liu, Y., Ding, Y., Liu, W., and Liu, J. (2021). Recent progress on protein-polyphenol complexes: Effect on stability and nutrients delivery of oil-in-water emulsion system. Front. Nutr., 8.","DOI":"10.3389\/fnut.2021.765589"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.tibs.2011.07.004","article-title":"The many blades of the beta-propeller proteins: Conserved but versatile","volume":"36","author":"Chen","year":"2011","journal-title":"Trends Biochem. Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"131278","DOI":"10.1016\/j.foodchem.2021.131278","article-title":"Caffeoyl substitution decreased the binding and inhibitory activity of quinic acid against \u03b1-amylase: The reason why chlorogenic acid is a relatively weak enzyme inhibitor","volume":"371","author":"Song","year":"2022","journal-title":"Food Chem."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Masson, P., and Lushchekina, S. (2022). Conformational stability and denaturation processes of proteins investigated by electrophoresis under extreme conditions. Molecules, 27.","DOI":"10.3390\/molecules27206861"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1021\/acsinfecdis.7b00003","article-title":"Exploring covalent allosteric inhibition of antigen 85C from mycobacterium tuberculosis by ebselen derivatives","volume":"3","author":"Goins","year":"2017","journal-title":"ACS Infect. Dis."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"109821","DOI":"10.1016\/j.foodhyd.2024.109821","article-title":"Molecular interactions between polyphenols and porcine \u03b1-amylase: An inhibition study on starch granules probed by kinetic, spectroscopic, calorimetric and in silico techniques","volume":"151","author":"Le","year":"2024","journal-title":"Food Hydrocoll."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1517\/17460441.2013.806479","article-title":"Recent developments in the use of differential scanning fluorometry in protein and small molecule discovery and characterization","volume":"8","author":"Simeonov","year":"2013","journal-title":"Expert. Opin. Drug Discov."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"111210","DOI":"10.1016\/j.foodres.2022.111210","article-title":"Alpha-amylase inhibition of a certain dietary polyphenol is predominantly affected by the concentration of alpha-1, 4-glucosidic bonds in starchy and artificial substrates","volume":"157","author":"Zhang","year":"2022","journal-title":"Food Res. Int."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"103753","DOI":"10.1016\/j.sjbs.2023.103753","article-title":"Molecular dynamics and simulation analysis against superoxide dismutase (SOD) target of micrococcus luteus with secondary metabolites from bacillus licheniformis recognized by genome mining approach","volume":"30","author":"Bagewadi","year":"2023","journal-title":"Saudi J. Biol. Sci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"122251","DOI":"10.1016\/j.saa.2022.122251","article-title":"Inhibitory mechanism of phenolic compounds in rapeseed oil on \u03b1-amylase and \u03b1-glucosidase: Spectroscopy, molecular docking, and molecular dynamic simulation","volume":"289","author":"Liu","year":"2023","journal-title":"Spectrochim. Acta Part A Mol. Biomol. Spectrosc."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"121797","DOI":"10.1016\/j.saa.2022.121797","article-title":"Structure-activity relationships and the underlying mechanism of \u03b1-amylase inhibition by hyperoside and quercetin: Multi-spectroscopy and molecular docking analyses","volume":"285","author":"Shen","year":"2023","journal-title":"Spectrochim. Acta Part A Mol. Biomol. Spectrosc."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"e202402984","DOI":"10.1002\/slct.202402984","article-title":"Inhibitory mechanisms of \u03b2-glucuronidase by hibiscus syriacus phenolics: Integrating computational and experimental approaches","volume":"10","author":"Alqhtani","year":"2025","journal-title":"ChemistrySelect"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"108938","DOI":"10.1016\/j.jmgm.2024.108938","article-title":"Molecular interaction profiling and binding dynamics of cinnamomum zeylanicum phytochemicals with human pancreatic amylase","volume":"136","author":"Rao","year":"2025","journal-title":"J. Mol. Graph. 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