4.8 Article

Nanoscale View of Amyloid Photodynamic Damage

期刊

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 142, 期 2, 页码 922-930

出版社

AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b10632

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资金

  1. Japan-Spain Joint Funding in Nanomedicine program (AMYLIGHT, Japan Agency for Medical Research and Development) [JP19jm0210058]
  2. Japan -Spain Joint Funding in Nanomedicine program (Ministerio de Ciencia, InnovaciOn y Universidades) [PCI2018-093064]
  3. IMDEA Nanociencia [PGC2018-094802-B-I00, CTQ2016-78454-C2-1-R, SAF2017-87305-R, SEV-2016-0686]
  4. Comunidad Autonoma de Madrid [S2017/BMD-3867, PEJD-2016/IND-2774]
  5. JSPS KAKENHI [JP16H06216, JP17H01522, JP17K19479, JP19K22484]
  6. Terumo Life Science Foundation

向作者/读者索取更多资源

A combination of time-resolved optical spectroscopy and nanoscale imaging has been used to study the complex binding to amyloids of a photocatalyst that selectively photo-oxygenates pathogenic aggregates, as well as the consequences of its irradiation. Correlative atomic force microscopy (AFM) and fluorescence microscopy reveals topography-dependent binding of the dye to model beta-lactoglobulin fibers, which may also explain the observed difference in their response to photodegradation. We provide direct evidence of the photosensitization of singlet oxygen by the photocatalyst bound to amyloid fibers by direct detection of its NIR phosphorescence. The effect of singlet oxygen at the molecular level brings about nanoscale morphological changes that can be observed with AFM at the single-fiber level. We also find differential response of two a-synuclein mutants to photodamage, which can be rationalized by the presence of amino acids susceptible to photo-oxygenation. Overall, our results help to unravel some of the complexity associated with highly heterogeneous amyloid populations and contribute to the development of improved phototherapeutic strategies for amyloid-related disorders.

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