Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid β (Aβ) peptides in the monomer and protofibril states

@article{Algamal2017AtomicresolutionMO,
  title={Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid β (Aβ) peptides in the monomer and protofibril states},
  author={Moustafa Algamal and Rashik Ahmed and Naeimeh Jafari and Bilal Ahsan and Joaquin Ortega and Giuseppe Melacini},
  journal={The Journal of Biological Chemistry},
  year={2017},
  volume={292},
  pages={17158 - 17168}
}
Self-association of amyloid β (Aβ) peptides is a hallmark of Alzheimer's disease and serves as a general prototype for amyloid formation. A key endogenous inhibitor of Aβ self-association is human serum albumin (HSA), which binds ∼90% of plasma Aβ. However, the exact molecular mechanism by which HSA binds Aβ monomers and protofibrils is not fully understood. Here, using dark-state exchange saturation transfer NMR and relaxation experiments complemented by morphological characterization, we… CONTINUE READING

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