pH-dependent binding of synthetic beta-amyloid peptides to glycosaminoglycans

Topic: Brain proteins, microglia and lab models

The senile plaques found within the cerebral cortex and hippocampus of the Alzheimer disease brain contain beta-amyloid peptide (A beta) fibrils that are associated with a variety of macromolecular species, including dermatan sulfate proteoglycan and heparan sulfate proteoglycan. The latter has been shown recently to bind tightly to both amyloid precursor protein and A beta, and this binding has been attributed largely to the interaction of the core protein of heparan sulfate proteoglycan with A beta and its precursor. Here we have examined the ability of synthetic A beta s to bind to and interact with the glycosaminoglycan moieties of proteoglycans.

@article{brunden1993-8245966,
  author  = {Brunden, K. R. and Richter-Cook, N. J. and Chaturvedi, N. and Frederickson, R. C.},
  title   = {{pH-dependent binding of synthetic beta-amyloid peptides to glycosaminoglycans}},
  journal = {Journal of neurochemistry},
  year    = {1993},
  doi     = {10.1111/j.1471-4159.1993.tb07453.x},
  pmid    = {8245966},
  url     = {https://doi.org/10.1111/j.1471-4159.1993.tb07453.x}
}

Key findings

• The latter has been shown recently to bind tightly to both amyloid precursor protein and A beta, and this binding has been attributed largely to the interaction of the core protein of heparan sulfate proteoglycan with A beta and its precursor.
• Here we have examined the ability of synthetic A beta s to bind to and interact with the glycosaminoglycan moieties of proteoglycans.
• A beta(1-28) associates with heparin, heparan sulfate, dermatan sulfate, and chondroitin sulfate.
• The interaction of these sulfated polysaccharides with the amyloid peptide results in the formation of large aggregates that are readily sedimented by centrifugation.

Why it matters

This laboratory study examined how synthetic amyloid-beta peptides bind to glycosaminoglycans in a pH-dependent way. It is basic biochemistry work and does not test any treatment, cure or prevention for Alzheimer's disease.

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Study details

• Evidence strengthLow

Read the original

• DOI: 10.1111/j.1471-4159.1993.tb07453.x
• PubMed: 8245966
• Original source →

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• Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein Biochemical and Biophysical Research Communications · 1984-05-01 · usefulness score 54/100 · Disease mechanisms

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