Booth D R, Sunde M, Bellotti V, Robinson C V, Hutchinson W L, Fraser P E, Hawkins P N, Dobson C M, Radford S E, Blake C C, Pepys M B
Immunological Medicine Unit, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK.
Nature. 1997 Feb 27;385(6619):787-93. doi: 10.1038/385787a0.
Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
可溶性蛋白质以淀粉样纤维形式在组织中沉积是一系列致命疾病的基础。两种天然存在的人溶菌酶变体都具有淀粉样变性，并且在此显示为不稳定的。它们聚集形成淀粉样纤维，同时晶体结构中观察到的主要为螺旋状的天然折叠转变为淀粉样纤维的交叉β折叠。生物物理研究表明，部分折叠的中间体参与了纤维形成过程，这可能与一般的淀粉样变性有关。
