Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    FTIR studies of the similarities between pathology induced protein aggregation in vivo and chemically induced protein aggregation ex vivo

    Access Status
    Fulltext not available
    Authors
    Tidy, R.
    Lam, V.
    Fimognari, N.
    Mamo, John
    Hackett, M.
    Date
    2016
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Tidy, R. and Lam, V. and Fimognari, N. and Mamo, J. and Hackett, M. 2016. FTIR studies of the similarities between pathology induced protein aggregation in vivo and chemically induced protein aggregation ex vivo. Vibrational Spectroscopy. [In Press].
    Source Title
    Vibrational Spectroscopy
    DOI
    10.1016/j.vibspec.2016.09.016
    ISSN
    0924-2031
    School
    School of Public Health
    URI
    http://hdl.handle.net/20.500.11937/18066
    Collection
    • Curtin Research Publications
    Abstract

    © 2016 Elsevier B.V.Fourier transform infrared (FTIR) spectroscopy has been well documented to discriminate between protein secondary structures, at the micron scale. This capability has enabled in situ localization of ß-sheet aggregate accumulation within the central nervous system during pathological protein misfolding associated with Prion disease, Amyotrophic Lateral Sclerosis, Huntington's Disease, Alzheimer's' Disease, and Parkinson's Disease. In addition to the above diseases, similar spectral alterations occurring over the range ~1625-1630cm-1 have been reported in other biological systems, including inclusion body formation within bacteria and during the formation of high molecular weight protein aggregates via protein oxidation and denaturation. Thus, the characteristic spectral alterations to the amide-I band observed during protein misfolding in neurological disorders are likely not specific to these diseases, but rather, reflect an aggregated protein end point, which can result from a range of biochemical events. For example, a common pathogenic component of many neurological conditions is oxidative stress, protein oxidation and altered ion homeostasis, which have the potential to denature proteins and promote the formation of high molecular weight aggregates.Oxidative stress is a generic feature of neurodegenerative diseases and also occurs during neurodegenerative conditions, such as stroke, multiple sclerosis, epilepsy and cerebral malaria. These neuropathological disorders do not have an established protein misfolding pathology, in contrast to Prion disease, Amyotrophic Lateral Sclerosis, Huntington's Disease, Alzheimer's' Disease, which do have an established protein misfolding pathology. Interestingly, recent studies using FTIR have confirmed the presence of protein aggregates within the central nervous system during stroke, cerebral malaria, epilepsy, multiple sclerosis. Such reports suggest FTIR spectroscopy may be a highly valuable research tool to study protein aggregation as a marker of oxidative stress and neurodegeneration in many diseases, not just those with a characteristic pathology for protein misfolding. This manuscript extends the recent literature and reports further characterization of the alterations to the amide I band that result from ubiquitous . ex vivo protein aggregation in cerebral tissue. The new data presented highlights that the spectroscopic alterations to the amide I band often reported for amyloid-ß plaques in Alzheimer's disease, are spectroscopically very similar to spectroscopic alterations observed during ischemia induced neurodegeneration (stroke) and . ex vivo induced protein aggregation. As such, this study further validates FTIR as a useful platform to study protein aggregation in neurological disorders, including those not characterized by protein misfolding pathology.

    Related items

    Showing items related by title, author, creator and subject.

    • Nutritional and pharmacological regulation of cerebral capillary function
      Pallebage-Gamarallage, Menuka Madhavi Somapala (2012)
      Alzheimer’s disease (AD) is the most common cause of dementia pathologically characterised by neurovascular inflammation, extracellular proteinaceous deposits enriched in amyloid-β (Aβ) and formation of neurofibrillar ...
    • FTIR imaging of brain tissue reveals crystalline creatine deposits are an ex vivo marker of localized ischemia during murine cerebral malaria: General implications for disease neurochemistry
      Hackett, Mark; Lee, J.; El-Assaad, F.; McQuillan, J.; Carter, E.; Grau, G.; Hunt, N.; Lay, P. (2012)
      Phosphocreatine is a major cellular source of high energy phosphates, which is crucial to maintain cell viability under conditions of impaired metabolic states, such as decreased oxygen and energy availability (i.e., ...
    • In situ biospectroscopic investigation of rapid ischemic and postmortem induced biochemical alterations in the rat brain
      Hackett, Mark; Britz, C.; Paterson, P.; Nichol, H.; Pickering, I.; George, G. (2015)
      © 2014 American Chemical Society. Rapid advances in imaging technologies have pushed novel spectroscopic modalities such as Fourier transform infrared spectroscopy (FTIR) and X-ray absorption spectroscopy (XAS) at the ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.