Abstract
AbstractBackgroundIs amyloid formation an exothermic process with the potential to damage brain tissue by local hyperthermia? In our study we aim to find answers to the above question. Several proteins, i.e. lysozyme and amyloid‐β peptide, known to form amyloid structures are investigated primarily by differential scanning calorimetry (DSC) in order to determine their thermodynamic properties.MethodExperiments in DSC are complemented by a set of other biophysical methods in order to clarify molecular parameters for the evaluation of the heat capacity measurements.ResultFor this purpose a seeded amyloid formation assay has been designed. In this assay the structural conversion of a given amount of monomeric protein is accelerated and synchronized by the addition of preformed amyloid fibril fragments to result in reproducible heat bursts caused by amyloid formation.ConclusionFirst results are reported and the measured enthalpies are related to known enthalpies from protein structural conversion processes.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
