Selection and characterization of Affibody ligands binding to Alzheimer amyloid beta peptides

Topic: Amyloid, tau and blood-test diagnosis

Affibody (Affibody) ligands specific for human amyloid beta (Abeta) peptides (40 or 42 amino acid residues in size), involved in the progress of Alzheimer's disease, were selected by phage display technology from a combinatorial protein library based on the 58-amino acid residue staphylococcal protein A-derived Z domain. Post-selection screening of 384 randomly picked clones, out of which 192 clones were subjected to DNA sequencing and clustering, resulted in the identification of 16 Affibody variants that were produced and affinity purified for ranking of their binding properties. The two most promising Affibody variants were shown to selectively and efficiently bind to Abeta peptides, but not to the control proteins.

Key findings

• Post-selection screening of 384 randomly picked clones, out of which 192 clones were subjected to DNA sequencing and clustering, resulted in the identification of 16 Affibody variants that were produced and affinity purified for ranking of their binding properties.
• The two most promising Affibody variants were shown to selectively and efficiently bind to Abeta peptides, but not to the control proteins.
• These two Affibody ligands were in dimeric form (to gain avidity effects) coupled to affinity resins for evaluation as affinity devices for capture of Abeta peptides from human plasma and serum.
• It was found that both ligands could efficiently capture Abeta that were spiked (100 microgml(-1)) to plasma and serum samples.

Why it matters

Researchers selected Affibody ligands that bind selectively to human amyloid-beta peptides in the laboratory. This is an early laboratory study and does not demonstrate any treatment, cure, or prevention for Alzheimer's disease.

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Study details

• Evidence strengthLow

Read the original

• DOI: 10.1016/j.jbiotec.2006.09.013
• PubMed: 17088007
• Original source →

May need a subscription OpenAlex found no free copy of the full text (checked 6 Feb 1020), so the publisher may charge for it. The PubMed abstract is free.

@article{gronwall2007-17088007,
  author  = {Grönwall, C. and Jonsson, A. and Lindström, S. and Gunneriusson, E. and Ståhl, S. and Herne, N.},
  title   = {{Selection and characterization of Affibody ligands binding to Alzheimer amyloid beta peptides}},
  journal = {Journal of biotechnology},
  year    = {2007},
  doi     = {10.1016/j.jbiotec.2006.09.013},
  pmid    = {17088007},
  url     = {https://doi.org/10.1016/j.jbiotec.2006.09.013}
}

Studies this one cites

Referenced by this study and also in the alzhub library, so you can read them here.

• The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics Science · 2002-07-19 · usefulness score 65/100 · Disease mechanisms
• Alzheimer's Disease: Genes, Proteins, and Therapy Physiological Reviews · 2001-04-01 · usefulness score 58/100 · Disease mechanisms

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• Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease The Journal of biological chemistry · 1994-04-01 · usefulness score 43/100
• Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease Journal of peptide science : an official publication of the European Peptide Society · 2004-05-01 · usefulness score 41/100
• Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease Current protein & peptide science · 2004-02-01 · usefulness score 38/100

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