Membrane Disruption Mechanism of a Prion Peptide (106–126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy
作者： Jianjun Pan , Prasana K. Sahoo , Annalisa Dalzini , Zahra Hayati , Chinta M. Aryal
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摘要: A fragment of the human prion protein spanning residues 106–126 (PrP106–126) recapitulates many essential properties disease-causing such as amyloidogenicity and cytotoxicity. PrP106–126 has an amphipathic characteristic that resembles antimicrobial peptides (AMPs). Therefore, toxic effect could arise from a direct association monomeric with membrane matrix. Several experimental approaches are employed to scrutinize impacts on model lipid membranes. Porous defects in planar bilayers observed by using solution atomic force microscopy. Adding cholesterol does not impede defect formation. spectroscopy experiment shows reduces Young’s modulus bilayers. We use Raman microspectroscopy study vibrational dynamics. For phosphatidylcholine lipids, disorders intrachain conformation, while interchain interaction is altered; for...
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