Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptide

Conversion of amyloid fibrils by many peptides/proteins involves cytotoxic helix-rich oligomers. However, their toxicity and biophysical studies remain largely unknown due to their highly dynamic nature. To address this, we chose two helical peptides (melittin, Mel and pancreatic polypeptide, PP) an...

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Veröffentlicht in:	PloS one 2015-03, Vol.10 (3), p.e0120346
Hauptverfasser:	Singh, Pradeep K, Ghosh, Dhiman, Tewari, Debanjan, Mohite, Ganesh M, Carvalho, Edmund, Jha, Narendra Nath, Jacob, Reeba S, Sahay, Shruti, Banerjee, Rinti, Bera, Amal K, Maji, Samir K
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer's disease Amyloid - chemistry Amyloid - metabolism Amyloidogenesis Animals Anticoagulants Apoptosis Bees Biochemistry Bioengineering Cell death Cell Line Cytotoxicity Diabetes Fibrils Heparin Heparin - metabolism Humans Hydrophobicity Intermediates Lipids Melitten - chemistry Melitten - metabolism Models, Molecular Neurons - cytology Neurons - metabolism Neurotoxins - chemistry Neurotoxins - metabolism Oligomerization Oligomers Pancreatic Polypeptide - chemistry Pancreatic Polypeptide - metabolism Parkinson's disease Peptides Polypeptides Pore formation Protein Aggregates Protein Structure, Secondary Proteins Random coil Studies Synuclein Toxicity
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