title: Nanoporous protein matrix made of amyloid fibrils of β2-microglobulin.
abstract: Amyloid fibrils are considered as novel nanomaterials because of their nanoscale width, a regular constituting structure of cross β-sheet conformation, and considerable mechanical strength. By using an amyloidogenic protein of β(2)-microglobulin (β(2)M) related to dialysis-related amyloidosis, nanoporous protein matrix has been prepared. The β(2) M granules made of around 15 monomers showed an average size of 23.1 nm. They formed worm-like fibrils at pH 7.4 in 20 mM sodium phosphate containing 0.15 M NaCl following vigorous nondirectional shaking incubation, in which they became laterally associated and interwound to generate the porous amyloid fibrillar matrix with an average pore size of 30-50 nm. This nanoporous protein matrix was demonstrated to be selectively disintegrated by reducing agents, such as tris-(2-carboxyethyl) phosphine. High surface area with nanopores on the surface has been suggested to make the matrix of β(2) M amyloid fibrils particularly suitable for applications in the area of nanobiotechnology including drug delivery and tissue engineering.
authors.affiliation: School of Chemical and Biological Engineering, College of Engineering, Seoul National University, Seoul 151-744, Korea.
authors.forename: Minkoo
authors.initials: M
authors.lastname: Ahn
authors.forename: Sungsoo
authors.initials: S
authors.lastname: Kang
authors.forename: Hee Jung
authors.initials: HJ
authors.lastname: Koo
authors.forename: Jung-Ho
authors.initials: JH
authors.lastname: Lee
authors.forename: Yoon-Sik
authors.initials: YS
authors.lastname: Lee
authors.forename: Seung R
authors.initials: SR
authors.lastname: Paik
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D049329:Nanostructures / Q000737:chemistry*; D016062:Porosity; D013499:Surface Properties; D001613:beta 2-Microglobulin / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D000682:Amyloid; D001613:beta 2-Microglobulin