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Amyloid fragments and their toxicity on neural cells

Regenerative Biomaterials 2019年第2期6卷 121-127页

作者： Eva Bystrenova zuzana Bednarikova Marianna Barbalinardo Cristiano Albonetti Francesco Valle zuzana gazova Institute of Nanostructured Materials I.S.M.N–C.N.R. via Gobetti101Bologna 40129Italy Department of Biophysics Institute of Experimental Physics SASWatsonova 47Kosice 04353Slovakia

The formation of amyloid fibrils from soluble proteins is a common form of self-assembly phenomenon that has fundamental connections with biological functions and human *** was converted from its soluble native state into highly organized amyloid *** treatment was used to break amyloid fibrils to fibrillar fragments–*** force microscopy and fluorescence microscopy was employed to characterize the morphology of the amyloid assemblies and neural cells–amyloid *** results demonstrate that prefibrillar intermediated and their mixture with proteins exhibit toxicity,although native proteins and fibrils appear to have no effect on number of *** findings confirm that innocuous hen lysozyme can be engineered to produce both cytotoxic fibrillar fragments and non-toxic mature amyloid *** work further strengthens the claim that amyloid conformation,and not the identity of the protein,is key to cellular toxicity and the underlying specific cell death mechanism.

关键词： amyloid fibrils protein aggregation neural cells atomic force microscopy fluorescence microscopy

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Effect of metallic nanoparticles on amyloid fibrils and their influence to neural cell toxicity

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Nano Research 2020年第4期13卷 1081-1089页

作者： Marianna Barbalinardo Andrea Antosova Marta Gambucci zuzana Bednarikova Cristiano Albonetti Francesco Valle Paola Sassi Loredana Latterini(ISI) zuzana gazova Eva Bystrenova C.N.R.-I.S.M.N via gobetti101bologna 40129italy Institute of experimental physics department of biophysicsslovak academy of sciencewatsonova 4704001kosiceslovakia department of chemistry biology and biotechnologyuniversity of perugiaperugia 06123italy consorzio interuniversitario per lo sviluppo dei sistemi a grande interfase(csgi) ismn-cnrbologna 40129italy department of medical and clinical biochemistry faculty of medicinesafarik universitykosice 04001slovakia

The modification of amyloid fibrils cytotoxicity through exogenous nanomaterials is crucial to understand the processes controlling the role of protein aggregation in the related *** influence of nanoparticles on amyloid stability yields great interest due to the small size and high surface area-to-volume ratio of *** physico-chemical parameters play a role in the interaction of proteins and nanoparticles in solution,thus influencing the disaggregation of preformed *** have examined the influence of two kinds of metallic nanoparticles on lysozyme amyloid fibrils using a multi-technique approach and focalized their impact on cytotoxicity on human neuroblastoma cells(SH-SY5Y).In particular,fluorescence,infrared and circular dichroism spectroscopies,optical and atomic force microscopy experiments have been carried out;the results are analyzed to rationalize the effects of these complexes on neural cell *** is remarkable,that the fibrils in the presence of AuNPs,unlike fibrils alone or with AgNPs,do not generate a significant cytotoxic effect even at high concentration and an amyloid degradation effect is visible.

关键词： lysozyme amyloid fibrils nanoparticles spectroscopy toxicity

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