{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T03:37:21Z","timestamp":1788406641070,"version":"build-2803163510"},"reference-count":61,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2024,12,9]],"date-time":"2024-12-09T00:00:00Z","timestamp":1733702400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["105-2320-B-039-036-MY3"],"award-info":[{"award-number":["105-2320-B-039-036-MY3"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004663","name":"Ministry of Science and Technology, Taiwan","doi-asserted-by":"publisher","award":["CMU105-ASIA-07"],"award-info":[{"award-number":["CMU105-ASIA-07"]}],"id":[{"id":"10.13039\/501100004663","id-type":"DOI","asserted-by":"publisher"}]},{"name":"China Medical University, Asia University, Taiwan","award":["105-2320-B-039-036-MY3"],"award-info":[{"award-number":["105-2320-B-039-036-MY3"]}]},{"name":"China Medical University, Asia University, Taiwan","award":["CMU105-ASIA-07"],"award-info":[{"award-number":["CMU105-ASIA-07"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Alzheimer\u2019s disease (AD), a leading neurodegenerative disorder, is closely associated with the accumulation of amyloid-beta (A\u03b2) peptides in the brain. The enzyme \u03b2-secretase (BACE1), pivotal in A\u03b2 production, represents a promising therapeutic target for AD. While bioactive peptides derived from food protein hydrolysates have neuroprotective properties, their inhibitory effects on BACE1 remain largely unexplored. In this study, we evaluated the inhibitory potential of protein hydrolysates from gliadin, whey, and casein proteins prepared using bromelain, papain, and thermolysin. Through in vitro and cellular assays, bromelain-hydrolyzed gliadin (G-Bro) emerged as the most potent BACE1 inhibitor, with an IC50 of 0.408 mg\/mL. G-Bro significantly reduced BACE1 expression and amyloid precursor protein (APP) processing in N2a\/PS\/APP cell cultures, suggesting its potential to attenuate A\u03b2 aggregation. The unique peptide profile of G-Bro likely contributes to its inhibitory effect, with proline residues disrupting \u03b2-sheets, lysine residues introducing positive charges that hinder aggregation, hydrophobic residues stabilizing binding interactions, and glutamine residues enhancing solubility and stability. These findings highlight gliadin hydrolysates, particularly G-Bro, as potential natural BACE1 inhibitors with applications in dietary interventions for AD prevention. However, further studies are warranted to elucidate specific peptide interactions and their bioactivity in neural pathways to better understand their therapeutic potential.<\/jats:p>","DOI":"10.3390\/ijms252313212","type":"journal-article","created":{"date-parts":[[2024,12,9]],"date-time":"2024-12-09T04:01:37Z","timestamp":1733716897000},"page":"13212","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Inhibitory Effects of Gliadin Hydrolysates on BACE1 Expression and APP Processing to Prevent A\u03b2 Aggregation"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2304-7381","authenticated-orcid":false,"given":"Chin-Yu","family":"Lin","sequence":"first","affiliation":[{"name":"Department of Biomedical Sciences and Engineering, Tzu Chi University, No. 701, Sec. 3, Zhongyang Rd., Hualien City 970374, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cheng-Hong","family":"Hsieh","sequence":"additional","affiliation":[{"name":"Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan"},{"name":"Department of Food Nutrition and Health Biotechnology, Asia University, 500 Lioufeng Rd., Wufeng, Taichung City 41354, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pei-Yu","family":"Lai","sequence":"additional","affiliation":[{"name":"Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ching-Wei","family":"Huang","sequence":"additional","affiliation":[{"name":"Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yung-Hui","family":"Chung","sequence":"additional","affiliation":[{"name":"Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shang-Ming","family":"Huang","sequence":"additional","affiliation":[{"name":"Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3449-8447","authenticated-orcid":false,"given":"Kuo-Chiang","family":"Hsu","sequence":"additional","affiliation":[{"name":"Department of Nutrition, China Medical University, No. 100, Sec. 1, Jingmao Rd., Beitun Dist., Taichung City 40604, Taiwan"},{"name":"Department of Food Nutrition and Health Biotechnology, Asia University, 500 Lioufeng Rd., Wufeng, Taichung City 41354, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,12,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Adem, M.A., Decourt, B., and Sabbagh, M.N. (2024). Pharmacological Approaches Using Diabetic Drugs Repurposed for Alzheimer\u2019s Disease. Biomedicines, 12.","DOI":"10.3390\/biomedicines12010099"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"105761","DOI":"10.1016\/j.neuint.2024.105761","article-title":"Advances in Alzheimer\u2019s disease: A multifaceted review of potential therapies and diagnostic techniques for early detection","volume":"177","author":"Sharma","year":"2024","journal-title":"Neurochem. Int."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Raymond, R.D.D. (2024). Biomedicines in Longevity and Aging The Quest to Resist Biological Decline. BioMedicine, 14.","DOI":"10.37796\/2211-8039.1433"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1038\/s12276-023-01146-2","article-title":"Current understanding of the Alzheimer\u2019s disease-associated microbiome and therapeutic strategies","volume":"56","author":"Seo","year":"2024","journal-title":"Exp. Mol. Med."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Sharma, M., Tanwar, A.K., Purohit, P.K., Pal, P., Kumar, D., Vaidya, S., Prajapati, S.K., Kumar, A., Dhama, N., and Kumar, S. (2024). Regulatory roles of microRNAs in modulating mitochondrial dynamics, amyloid beta fibrillation, microglial activation, and cholinergic signaling: Implications for Alzheimer\u2019s disease pathogenesis. Neurosci. Biobehav. Rev., 161.","DOI":"10.1016\/j.neubiorev.2024.105685"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/s40035-024-00434-9","article-title":"Trajectory of brain-derived amyloid beta in Alzheimer\u2019s disease: Where is it coming from and where is it going?","volume":"13","author":"Liu","year":"2024","journal-title":"Transl. Neurodegener."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/j.jconrel.2016.06.001","article-title":"Messenger RNA-based therapeutics for brain diseases: An animal study for augmenting clearance of beta-amyloid by intracerebral administration of neprilysin mRNA loaded in polyplex nanomicelles","volume":"235","author":"Lin","year":"2016","journal-title":"J. Control. Release"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"369","DOI":"10.4103\/apjtb.apjtb_192_24","article-title":"BACE1 inhibitors: A promising therapeutic approach for the management of Alzheimer\u2019s disease","volume":"14","author":"Arya","year":"2024","journal-title":"Asian Pac. J. Trop. Biomed."},{"key":"ref_9","first-page":"1","article-title":"BACE1 Inhibitors for Alzheimer\u2019s Disease: Current Challenges and Future Perspectives","volume":"101","author":"Coimbra","year":"2024","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"105327","DOI":"10.1016\/j.ebiom.2024.105327","article-title":"Clinical and research application of fluid biomarkers in autosomal dominant Alzheimer\u2019s disease and Down syndrome","volume":"108","author":"Lao","year":"2024","journal-title":"EBioMedicine"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Chen, X., Drew, J., Berney, W., and Lei, W. (2021). Neuroprotective Natural Products for Alzheimer\u2019s Disease. Cells, 10.","DOI":"10.3390\/cells10061309"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"881","DOI":"10.2174\/1389557523666221118113923","article-title":"Natural Products with BACE1 and GSK3\u03b2 Inhibitory Activity","volume":"23","author":"Prado","year":"2023","journal-title":"Mini-Rev. Med. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2967","DOI":"10.1007\/s11030-023-10726-3","article-title":"Identifying \u03b2-secretase 1 (BACE1) inhibitors from plant-based compounds: An approach targeting Alzheimer\u2019s therapeutics employing molecular docking and dynamics simulation","volume":"28","author":"Alrouji","year":"2023","journal-title":"Mol. Divers."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2620","DOI":"10.3168\/jds.2023-24284","article-title":"Neuroprotective effect of whey protein hydrolysate containing leucine-aspartate-isoleucine-glutamine-lysine on HT22 cells in hydrogen peroxide\u2013induced oxidative stress","volume":"107","author":"Chang","year":"2024","journal-title":"J. Dairy Sci."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Han, D., Li, A., Zhu, L., Zhuang, C., Zhao, Q., and Zou, Y. (2024). Peptide inhibitors targeting Ras and Ras-associated protein\u2013protein interactions. Eur. J. Med. Chem., 116878.","DOI":"10.1016\/j.ejmech.2024.116878"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1789","DOI":"10.1007\/s10068-024-01554-8","article-title":"Review of fish protein hydrolysates: Production methods, antioxidant and antimicrobial activity and nanoencapsulation","volume":"33","author":"Nemati","year":"2024","journal-title":"Food Sci. Biotechnol."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Sun, W., Shahrajabian, M.H., Kuang, Y., and Wang, N. (2024). Amino acids biostimulants and protein hydrolysates in agricultural sciences. Plants, 13.","DOI":"10.3390\/plants13020210"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1974","DOI":"10.26599\/FSHW.2022.9250164","article-title":"Antihypertensive effects of whey protein hydrolysate involve reshaping the gut microbiome in spontaneously hypertension rats","volume":"13","author":"Dou","year":"2024","journal-title":"Food Sci. Hum. Wellness"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Ding, N., Meng, H., Wu, C., Hong, H., Luo, Y., and Tan, Y. (2024). Targeting brain health: Whey protein hydrolysate intervention enhances cognitive function in middle-aged mice. Food Biosci., 57.","DOI":"10.1016\/j.fbio.2023.103460"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1007\/s00394-023-03267-w","article-title":"Collagen peptide supplementation before bedtime reduces sleep fragmentation and improves cognitive function in physically active males with sleep complaints","volume":"63","author":"Thomas","year":"2024","journal-title":"Eur. J. Nutr."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"125347","DOI":"10.1016\/j.talanta.2023.125347","article-title":"Measurement of degree of hydrolysis and molecular weight distribution of protein hydrolysates by liquid chromatography-mass spectrometry","volume":"268","author":"Zhao","year":"2024","journal-title":"Talanta"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"132632","DOI":"10.1016\/j.jhazmat.2023.132632","article-title":"Biodegradation of poly (ethylene terephthalate) through PETase surface-display: From function to structure","volume":"461","author":"Han","year":"2024","journal-title":"J. Hazard. Mater."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1039\/D4FB00085D","article-title":"Enzymatic modification of cold pressed coconut meal protein: Nutritional, functional and biological properties","volume":"2","author":"Akbarbaglu","year":"2024","journal-title":"Sustain. Food Technol."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Yeerong, K., Chantawannakul, P., Anuchapreeda, S., Wangtueai, S., and Chaiyana, W. (2024). Optimization of Hydrolysis Conditions, Isolation, and Identification of Biologically Active Peptides Derived from Acheta domesticus for Antioxidant and Collagenase Inhibition. Antioxidants, 13.","DOI":"10.3390\/antiox13030367"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Wang, C., Zheng, L., Udenigwe, C.C., Lin, L., and Zhao, M. (2024). Enzymatic characterization and synergistic effects of protease combinations on DPP-IV inhibitory peptide release from bovine casein. Food Biosci., 60.","DOI":"10.1016\/j.fbio.2024.104276"},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Nu\u00f1ez, S.M., Valencia, P., Sol\u00eds, T., Valdivia, S., C\u00e1rdenas, C., Guzman, F., Pinto, M., and Almonacid, S. (2024). Enzymatic Hydrolysis of Salmon Frame Proteins Using a Sequential Batch Operational Strategy: An Improvement in Water-Holding Capacity. Foods, 13.","DOI":"10.3390\/foods13091378"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1007\/s12649-023-02303-4","article-title":"Proteolysis coupled with membrane separation for the isolation of bioactive peptides from defatted smooth hound byproduct proteins","volume":"15","author":"Abdelhedi","year":"2024","journal-title":"Waste Biomass Valorizat."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"100487","DOI":"10.1016\/j.crfs.2023.100487","article-title":"Enzymatic hydrolysis of soy and chickpea protein with Alcalase and Flavourzyme and formation of hydrogen bond mediated insoluble aggregates","volume":"6","author":"Dent","year":"2023","journal-title":"Curr. Res. Food Sci."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.ijbiomac.2022.11.245","article-title":"Characterization of bacterial cellulose nanofibers\/soy protein isolate complex particles for Pickering emulsion gels: The effect of protein structure changes induced by pH","volume":"226","author":"Zhang","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.jcis.2024.04.136","article-title":"Influence of pH and lipid membrane on the liquid\u2013liquid phase separation of wheat \u03b3-gliadin in aqueous conditions","volume":"668","author":"Cochereau","year":"2024","journal-title":"J. Colloid Interface Sci."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Rani, M., Siddiqi, R.A., Sharma, R., Gill, B.S., and Sogi, D.S. (2023). Functional and structural properties of gliadin as influenced by pH, extraction protocols, and wheat cultivars. Int. J. Biol. Macromol., 234.","DOI":"10.1016\/j.ijbiomac.2023.123484"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"102342","DOI":"10.1016\/j.arr.2024.102342","article-title":"Navigating the Maze of Alzheimer\u2019s Disease by Exploring BACE1: Discovery, Current Scenario, and Future Prospects","volume":"98","author":"Iram","year":"2024","journal-title":"Ageing Res. Rev."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1080\/10408398.2020.1839855","article-title":"Bioactive functional ingredients from aquatic origin: A review of recent progress in marine-derived nutraceuticals","volume":"62","author":"Hosseini","year":"2022","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.procbio.2021.10.007","article-title":"Characterization and purification of \u03b2\u2212 secretase inhibitory peptides fraction from sea cucumber (Holothuria spinifera) enzymatic hydrolysates","volume":"111","author":"Rathnayake","year":"2021","journal-title":"Process Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Zhong, H., Jin, Y., Hussain, M., Liu, X., Feng, F., and Guan, R. (2024). Recent advances of hepatoprotective peptides: Production, structure, mechanisms, and interactions with intestinal microbiota. Food Biosci., 58.","DOI":"10.1016\/j.fbio.2024.103744"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1007\/s00044-024-03278-0","article-title":"Synthesis, in vitro activity, and molecular docking of caffeic acid and resveratrol derivatives against Alzheimer\u2019s disease-related enzymes","volume":"33","year":"2024","journal-title":"Med. Chem. Res."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Zhang, X.Q., Yu, Y., Sun, P., Fan, Z., Zhang, W.S., and Feng, C.Q. (2019). Royal jelly peptides: Potential inhibitors of \u03b2-secretase in N2a\/APP695swe cells. Sci. Rep., 9.","DOI":"10.1038\/s41598-018-35801-w"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Wang, J., Yu, Z., Peng, Y., and Xu, B. (2023). Insights into prevention mechanisms of bioactive components from healthy diets against Alzheimer\u2019s disease. J. Nutr. Biochem., 119.","DOI":"10.1016\/j.jnutbio.2023.109397"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"He, Z., Li, X., Wang, Z., Cao, Y., Han, S., Li, N., Cai, J., Cheng, S., and Liu, Q. (2023). Protective effects of luteolin against amyloid beta-induced oxidative stress and mitochondrial impairments through peroxisome proliferator-activated receptor \u03b3-dependent mechanism in Alzheimer\u2019s disease. Redox Biol., 66.","DOI":"10.1016\/j.redox.2023.102848"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1007\/s43440-024-00610-8","article-title":"Luteolin for neurodegenerative diseases: A review","volume":"76","author":"Jayawickreme","year":"2024","journal-title":"Pharmacol. Rep."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2582","DOI":"10.4103\/1673-5374.373680","article-title":"The role of natural flavonoids on neuroinflammation as a therapeutic target for Alzheimer\u2019s disease: A narrative review","volume":"18","author":"Zhang","year":"2023","journal-title":"Neural Regen. Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"52","DOI":"10.53388\/TMR20240209001","article-title":"Puerarin modulation of CENPA affects downstream PLK1 and CCNB1 expression to inhibit bladder cancer cell proliferation","volume":"9","author":"Xu","year":"2024","journal-title":"Tradit. Med. Res."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"5643","DOI":"10.1093\/nar\/gkae318","article-title":"Transcription factor shapes chromosomal conformation and regulates gene expression in bacterial adaptation","volume":"52","author":"Chen","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1021\/acs.jpcb.2c07607","article-title":"Illustrating the effect of small molecules derived from natural resources on amyloid peptides","volume":"127","author":"Roy","year":"2023","journal-title":"J. Phys. Chem. B"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"106174","DOI":"10.1016\/j.foodhyd.2020.106174","article-title":"Amyloid aggregation of spin-labeled \u03b2-lactoglobulin. Part II: Identification of spin-labeled protein and peptide sequences after amyloid aggregation","volume":"112","author":"Lux","year":"2020","journal-title":"Food Hydrocoll."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1007\/s10989-019-09876-6","article-title":"Colostral proline-rich polypeptide complexes. Comparative study of the antioxidant properties, cytokine-inducing activity, and nitric oxide release of preparations produced by a laboratory and a large-scale method","volume":"26","author":"Bartoszewska","year":"2020","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1007\/s00894-021-04968-x","article-title":"Destabilization of the Alzheimer\u2019s amyloid-\u03b2 peptide by a proline-rich \u03b2-sheet breaker peptide: A molecular dynamics simulation study","volume":"27","author":"Kanchi","year":"2021","journal-title":"J. Mol. Model."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Daniecki, N.J., Bhatt, M.R., Yap, G.P., and Zondlo, N.J. (2022). Proline C\u2212 H Bonds as Loci for Proline Assembly via C\u2212 H\/O Interactions. ChemBioChem, 23.","DOI":"10.1002\/cbic.202200409"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1021\/acs.chemrev.0c00981","article-title":"Proteostasis of islet amyloid polypeptide: A molecular perspective of risk factors and protective strategies for type II diabetes","volume":"121","author":"Milardi","year":"2021","journal-title":"Chem. Rev."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1006\/bbrc.2002.6514","article-title":"Poly-l-lysine dissolves fibrillar aggregation of the Alzheimer \u03b2-amyloid peptide in vitro","volume":"291","author":"Nguyen","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3070","DOI":"10.1021\/jasms.4c00317","article-title":"Photochemical and Collision-Induced Cross-Linking in Stereochemically Distinct Scaffolds of Peptides and Nitrile Imines in Gas-Phase Ions","volume":"35","author":"Zhu","year":"2024","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"24405","DOI":"10.1021\/acs.langmuir.4c02972","article-title":"Efficiency Enhancement in Peptide Hydrogelators: The Crucial Role of Side Chain Hydrogen Bonding Over Aromatic \u03c0\u2013\u03c0 Interactions","volume":"40","author":"Unnikrishnan","year":"2024","journal-title":"Langmuir"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"e202400053","DOI":"10.1002\/tcr.202400053","article-title":"Challenges in Peptide Solubilization\u2013Amyloids Case Study","volume":"24","author":"Szulc","year":"2024","journal-title":"Chem. Rec."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Sheikh, A.M., Tabassum, S., Yano, S., Abdullah, F.B., Wang, R., Ikeue, T., and Nagai, A. (2024). A Cationic Zn-Phthalocyanine Turns Alzheimer\u2019s Amyloid \u03b2 Aggregates into Non-Toxic Oligomers and Inhibits Neurotoxicity in Culture. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25168931"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2397","DOI":"10.1021\/acs.biochem.4c00371","article-title":"Peptide-Based Strategies: Combating Alzheimer\u2019s Amyloid \u03b2 Aggregation through Ergonomic Design and Fibril Disruption","volume":"63","author":"Pariary","year":"2024","journal-title":"Biochemistry"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2401918","DOI":"10.1002\/adma.202401918","article-title":"Co-Assembled Nanoparticles toward Multi-Target Combinational Therapy of Alzheimer\u2019s Disease by Making Full Use of Molecular Recognition and Self-Assembly","volume":"36","author":"Li","year":"2024","journal-title":"Adv. Mater."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Jukovi\u0107, M., Ratkaj, I., Kalafatovic, D., and Bradshaw, N.J. (2024). Amyloids, amorphous aggregates and assemblies of peptides\u2014Assessing aggregation. Biophys. Chem., 308.","DOI":"10.1016\/j.bpc.2024.107202"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Zhao, D., Zhou, Y., Xing, F., Wang, H., and Zhou, J. (2024). Porous organic cage as an inhibitor of A\u03b242 peptide: A simulation study. Phys. Chem. Chem. Phys.","DOI":"10.1039\/D4CP03549F"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Rosales Hern\u00e1ndez, M.C., Olvera-Valdez, M., Velazquez Toledano, J., Mendieta Wejebe, J.E., Fragoso Morales, L.G., and Cruz, A. (2024). Exploring the Benzazoles Derivatives as Pharmacophores for AChE, BACE1, and as Anti-A\u03b2 Aggregation to Find Multitarget Compounds against Alzheimer\u2019s Disease. Molecules, 29.","DOI":"10.3390\/molecules29194780"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"e2311733121","DOI":"10.1073\/pnas.2311733121","article-title":"Helical sulfonyl-\u03b3-AApeptides modulating A\u03b2 oligomerization and cytotoxicity by recognizing A\u03b2 helix","volume":"121","author":"Liu","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"141154","DOI":"10.1016\/j.foodchem.2024.141154","article-title":"Innovative insights into the enzymatic hydrolysis of salmon milt: Structural and functional analysis influenced by protease type and enzymolysis time","volume":"463","author":"Wang","year":"2025","journal-title":"Food Chem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/23\/13212\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:50:11Z","timestamp":1760115011000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/23\/13212"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,12,9]]},"references-count":61,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["ijms252313212"],"URL":"https:\/\/doi.org\/10.3390\/ijms252313212","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,12,9]]}}}