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Nanoporous Protein Matrix Made of Amyloid Fibrils of β2-Microglobulin

机译：β2-微球蛋白淀粉样原纤维制成的纳米多孔蛋白基质

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摘要

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 β2-microglobulin (β2M) related to dialysis-related amyloidosis, nanoporous protein matrix has been prepared. The β2M 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 β2M amyloid fibrils particularly suitable for applications in the area of nanobiotechnology including drug delivery and tissue engineering.
机译：淀粉状蛋白原纤维由于其纳米级的宽度，β-片状交叉构象的规则结构和相当大的机械强度而被认为是新型的纳米材料。通过使用与透析相关的淀粉样变性有关的β2-微球蛋白（β2M）的淀粉样蛋白，制备了纳米孔蛋白基质。由约15种单体制成的β2M颗粒的平均粒径为23.1 nm。在剧烈的非定向摇动孵育后，它们在含有0.15 M NaCl的20 mM磷酸钠中，在pH 7.4时形成蠕虫状原纤维，在其中横向结合并交缠在一起，生成平均孔径为30-50 nm的多孔淀粉样原纤维基质。已证明该纳米孔蛋白质基质被还原剂例如三-（2-羧乙基）膦选择性地崩解。已经建议在表面上具有纳米孔的高表面积使β2M淀粉样蛋白原纤维的基质特别适合在包括药物递送和组织工程在内的纳米生物技术领域中应用。

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