title: The synergistic effect between KLVFF and self-assembly chaperones on both disaggregation of beta-amyloid fibrils and reducing consequent toxicity.
abstract: By combining KLVFF peptide and self-assembly chaperone we fabricate a new system to achieve the synchronization between Aβ fibril disaggregation and reducing toxicity of Aβ fragments (monomers or oligomers) that consequently formed. When the KLVFF peptides disaggregate fibrils into fragments, the hydrophobic domains of self-assembly chaperones promptly bind them at the same time. This binding blocks the re-aggregation of the fragments and their interaction with cells, and hence reduces the toxicity of these dangerous fragments.
authors.affiliation: Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China. shilinqi@nankai.edu.cn.
authors.forename: Aoting
authors.initials: A
authors.lastname: Qu
authors.affiliation: Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China. shilinqi@nankai.edu.cn and Tianjin Key Laboratory of Radiation Medicine and Molecular Nuclear Medicine, Institute of Radiation Medicine, Chinese Academy of Medical Science & Peking Union Medical College, Tianjin, 300192, P. R. China.
authors.forename: Fan
authors.initials: F
authors.lastname: Huang
authors.affiliation: Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China. shilinqi@nankai.edu.cn.
authors.forename: Ang
authors.initials: A
authors.lastname: Li
authors.affiliation: Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China. shilinqi@nankai.edu.cn.
authors.forename: Huiru
authors.initials: H
authors.lastname: Yang
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, 300071, P. R. China.
authors.forename: Hao
authors.initials: H
authors.lastname: Zhou
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, 300071, P. R. China.
authors.forename: Jiafu
authors.initials: J
authors.lastname: Long
authors.affiliation: Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, Nankai University, Tianjin 300071, P. R. China. shilinqi@nankai.edu.cn.
authors.forename: Linqi
authors.initials: L
authors.lastname: Shi
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000633:toxicity*; D004357:Drug Synergism; D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D018832:Molecular Chaperones / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology*; D010316:Particle Size; D066329:Protein Aggregates / Q000187:drug effects; D066263:Protein Aggregation, Pathological / Q000188:drug therapy*; D013499:Surface Properties
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D008823:Micelles; D018832:Molecular Chaperones; D009842:Oligopeptides; D066329:Protein Aggregates