Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate
作者： Neda Motamedi-Shad , Tommaso Garfagnini , Amanda Penco , Annalisa Relini , Federico Fogolari
DOI: 10.1038/NSMB.2286
关键词: Heparan sulfate 、 Native state 、 Acylphosphatase 、 Chemistry 、 Plasma protein binding 、 Extracellular 、 Biochemistry 、 Extracellular matrix 、 Amyloid 、 Protein structure
摘要: Many human diseases are caused by the conversion of proteins from their native state into amyloid fibrils that deposit in extracellular space. Heparan sulfate, a component matrix, is universally associated with deposits and promotes fibril formation. The formation cytotoxic prefibrillar oligomers challenging to study because its rapidity, transient appearance heterogeneity species generated. process even more complex agents such as heparan sulfate. Here we have used stopped-flow device coupled turbidometry detection monitor rapid muscle acylphosphatase varying sulfate protein concentrations. We also analyzed mutants 15 basic amino acids acylphosphatase, identifying residues primarily involved sulfate-induced oligomerization this tracing unprecedented molecular detail.
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