Epitaxial growth of peptide nanofilaments on inorganic surfaces: effects of interfacial hydrophobicity/hydrophilicity.
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Biomedical subjects
Publications and source records attributed to Hong-Jie Xu.
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In the last decade, x-ray phase contrast imaging (XPCI) has received considerable attention as a novel imaging technique, which has proved to be suitable for weakly absorbing materials such as biomedical samples and polymers. In this paper, the microstructures of traditional Chinese medicines (TCMs), which are used as judging criteria in the identification of TCMs, were investigated by XPCI based on a nano-focus x-ray tube. The results demonstrated that XPCI is a promising new method for the identification of TCMs, with advantages such as nondestructivity, no special sample preparation and suitability for thick samples.
Human alpha-synuclein is a presynaptic terminal protein and can form insoluble fibrils that are believed to play an important role in the pathogenesis of several neurodegenerative diseases such as Parkinson's disease, dementia with Lewy bodies and Lewy body variant of Alzheimer's disease. In this paper, in situ atomic force microscopy has been used to study the structural properties of alpha-synuclein fibrils in solution using two different atomic force microscopy imaging modes: tapping mode and contact mode. In the in situ contact mode atomic force microscopy experiments alpha-synuclein fibrils quickly broke into fragments, and a similar phenomenon was found using tapping mode atomic force microscopy in which alpha-synuclein fibrils were incubated with guanidine hydrochloride (0.6 M). The alpha-synuclein fibrils kept their original filamentous topography for over 1 h in the in situ tapping mode atomic force microscopy experiments. The present results provide indirect evidence on how beta-sheets assemble into alpha-synuclein fibrils on a nanometer scale.