{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sun Q"],"funding":["Ningbo municipal innovation team of life science and health","Swiss National Science Foundation","Ningbo Sci &amp;amp; Tech Project for Common Wealth","Ningbo Sci & Tech Project for Common Wealth","Zhejiang Key Laboratory of Pathophysiology","Open Project Program of State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology","National Natural Science Foundation of China","LiDakSum Marine Biopharmaceutical Development Fund, and the K. C. Wong Magna Fund in Ningbo University","Open Project Program of State Key Laboratory of Food Nutrition and Safety, Tianjin University of Science &amp;amp; Technology"],"pagination":["E121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6409607"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(2)"],"pubmed_abstract":["β-Amyloid (Aβ) is regarded as an important pathogenic target for Alzheimer's disease (AD), the most prevalent neurodegenerative disease. Aβ can assemble into oligomers and fibrils, and produce neurotoxicity. Therefore, Aβ aggregation inhibitors may have anti-AD therapeutic efficacies. It was found, here, that the marine-derived alkaloid, fascaplysin, inhibits Aβ fibrillization <i>in vitro</i>. Moreover, the new analogue, 9-methylfascaplysin, was designed and synthesized from 5-methyltryptamine. Interestingly, 9-methylfascaplysin is a more potent inhibitor of Aβ fibril formation than fascaplysin. Incubation of 9-methylfascaplysin with Aβ directly reduced Aβ oligomer formation. Molecular dynamics simulations revealed that 9-methylfascaplysin might interact with negatively charged residues of"],"journal":["Marine drugs"],"pubmed_title":["9-Methylfascaplysin Is a More Potent Aβ Aggregation Inhibitor than the Marine-Derived Alkaloid, Fascaplysin, and Produces Nanomolar Neuroprotective Effects in SH-SY5Y Cells."],"pmcid":["PMC6409607"],"funding_grant_id":["NA","201804","SKLFNS-KF-201806","81870853, 21576199, 21878234, 20903058, 81850410553","201806","2017C50042","2015C110026"],"pubmed_authors":["Xiao X","Cui W","Yan S","Yan X","Wang N","He S","Sun Q","Liang H","Naman CB","Ma J","Sang J","Liu F","Lin M"],"additional_accession":[]},"is_claimable":false,"name":"9-Methylfascaplysin Is a More Potent Aβ Aggregation Inhibitor than the Marine-Derived Alkaloid, Fascaplysin, and Produces Nanomolar Neuroprotective Effects in SH-SY5Y Cells.","description":"β-Amyloid (Aβ) is regarded as an important pathogenic target for Alzheimer's disease (AD), the most prevalent neurodegenerative disease. Aβ can assemble into oligomers and fibrils, and produce neurotoxicity. Therefore, Aβ aggregation inhibitors may have anti-AD therapeutic efficacies. It was found, here, that the marine-derived alkaloid, fascaplysin, inhibits Aβ fibrillization <i>in vitro</i>. Moreover, the new analogue, 9-methylfascaplysin, was designed and synthesized from 5-methyltryptamine. Interestingly, 9-methylfascaplysin is a more potent inhibitor of Aβ fibril formation than fascaplysin. Incubation of 9-methylfascaplysin with Aβ directly reduced Aβ oligomer formation. Molecular dynamics simulations revealed that 9-methylfascaplysin might interact with negatively charged residues of","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Feb","modification":"2026-05-04T15:16:28.724Z","creation":"2019-06-06T20:58:42Z"},"accession":"S-EPMC6409607","cross_references":{"pubmed":["30781608"],"doi":["10.3390/md17020121"]}}