A common mechanism underlying amyloid fibrillation and protein crystallization revealed by the effects of ultrasonication.

摘要: Protein crystals form in supersaturated solutions via a nucleation and growth mechanism. The amyloid fibrils of denatured proteins also This similarity suggests that, although protein are distinct their morphologies, both processes can be controlled similar manner. It has been established that ultrasonication markedly accelerates the formation simultaneously breaks them down into fragmented fibrils. In this study, we investigated effects on crystallization hen egg white lysozyme glucose isomerase from Streptomyces rubiginosus. was monitored by light scattering, tryptophan fluorescence, transmittance. Repeated ultrasonic irradiations caused after cycles irradiations. size ultrasonication-induced small homogeneous, numbers were larger than those obtained under quiescent conditions. Switching off irradiation when scattering or fluorescence began to change resulted due suppression further fractures preformed crystals. results indicate fibrillation explained basis common phase diagram which crystal-like as well fragmentation