Somatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers. Wang, H., Muiznieks, L., Ghosh, P., Williams, D., Solarski, M., Fang, A., Ruiz-Riquelme, A., Pomès, R., Watts, J., Chakrabartty, A., Wille, H., Sharpe, S., & Schmitt-Ulms, G. eLife, 2017. doi abstract bibtex © 2017. Verasztó et al. The amyloid β peptide (Aβ) is a key player in the etiology of Alzheimer disease (AD), yet a systematic investigation of its molecular interactions has not been reported. Here we identified by quantitative mass spectrometry proteins in human brain extract that bind to oligomeric Aβ1-42 (oAβ1-42) and/or monomeric Aβ1-42 (mAβ1-42) baits. Remarkably, the cyclic neuroendocrine peptide somatostatin-14 (SST14) was observed to be the most selectively enriched oAβ1-42 binder. The binding interface comprises a central tryptophan within SST14 and the N-terminus of Aβ1-42. The presence of SST14 inhibited Aβ aggregation and masked the ability of several antibodies to detect Aβ. Notably, Aβ1-42, but not Aβ1-40, formed in the presence of SST14 oligomeric assemblies of 50 to 60 kDa that were visualized by gel electrophoresis, nanoparticle tracking analysis and electron microscopy. These findings may be relevant for Ab- directed diagnostics and may signify a role of SST14 in the etiology of AD.
@article{
title = {Somatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers},
type = {article},
year = {2017},
volume = {6},
id = {8ff5f184-8461-3f0f-bcda-23c70bc77e1f},
created = {2018-06-08T17:39:28.344Z},
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abstract = {© 2017. Verasztó et al. The amyloid β peptide (Aβ) is a key player in the etiology of Alzheimer disease (AD), yet a systematic investigation of its molecular interactions has not been reported. Here we identified by quantitative mass spectrometry proteins in human brain extract that bind to oligomeric Aβ1-42 (oAβ1-42) and/or monomeric Aβ1-42 (mAβ1-42) baits. Remarkably, the cyclic neuroendocrine peptide somatostatin-14 (SST14) was observed to be the most selectively enriched oAβ1-42 binder. The binding interface comprises a central tryptophan within SST14 and the N-terminus of Aβ1-42. The presence of SST14 inhibited Aβ aggregation and masked the ability of several antibodies to detect Aβ. Notably, Aβ1-42, but not Aβ1-40, formed in the presence of SST14 oligomeric assemblies of 50 to 60 kDa that were visualized by gel electrophoresis, nanoparticle tracking analysis and electron microscopy. These findings may be relevant for Ab- directed diagnostics and may signify a role of SST14 in the etiology of AD.},
bibtype = {article},
author = {Wang, H. and Muiznieks, L.D. and Ghosh, P. and Williams, D. and Solarski, M. and Fang, A. and Ruiz-Riquelme, A. and Pomès, R. and Watts, J.C. and Chakrabartty, A. and Wille, H. and Sharpe, S. and Schmitt-Ulms, G.},
doi = {10.7554/eLife.28401},
journal = {eLife}
}
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Verasztó et al. The amyloid β peptide (Aβ) is a key player in the etiology of Alzheimer disease (AD), yet a systematic investigation of its molecular interactions has not been reported. Here we identified by quantitative mass spectrometry proteins in human brain extract that bind to oligomeric Aβ1-42 (oAβ1-42) and/or monomeric Aβ1-42 (mAβ1-42) baits. Remarkably, the cyclic neuroendocrine peptide somatostatin-14 (SST14) was observed to be the most selectively enriched oAβ1-42 binder. The binding interface comprises a central tryptophan within SST14 and the N-terminus of Aβ1-42. The presence of SST14 inhibited Aβ aggregation and masked the ability of several antibodies to detect Aβ. Notably, Aβ1-42, but not Aβ1-40, formed in the presence of SST14 oligomeric assemblies of 50 to 60 kDa that were visualized by gel electrophoresis, nanoparticle tracking analysis and electron microscopy. 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