title: Fibril aggregates formed by a glatiramer-mimicking random copolymer of amino acids.
abstract: Amyloid formation is now considered a universal and intrinsic property of all proteins, irrespective of their sequences. Therefore, it is interesting to see whether random copolymers of amino acids can also form amyloid aggregates. Here we use a copolymer of 4 amino acids, mimicking the clinically used drug Glatiramer, and demonstrate that it does form amyloid-like fibrils in the aqueous solution despite its random sequence structure. The fibrillar aggregates show an alanine-rich β-sheet secondary structure, proving the high tolerance of amyloid aggregates to the sequence irregularity in poly(amino acid)s, and suggesting the potential application of random copolymers as amyloid materials.
authors.affiliation: Key Laboratory of Advanced Materials (MOE), Department of Chemical Engineering, Tsinghua University , Beijing 100084, China.
authors.forename: Jingjing
authors.initials: J
authors.lastname: Lai
authors.forename: Wenxin
authors.initials: W
authors.lastname: Fu
authors.forename: Lin
authors.initials: L
authors.lastname: Zhu
authors.forename: Ruohai
authors.initials: R
authors.lastname: Guo
authors.forename: Dehai
authors.initials: D
authors.lastname: Liang
authors.forename: Zhibo
authors.initials: Z
authors.lastname: Li
authors.forename: Yanbin
authors.initials: Y
authors.lastname: Huang
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D011108:Polymers