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A\u03b2 aggregation produces amyloid assemblies, such as oligomers and fibrils. In contrast to non-toxic A\u03b2 monomers, A\u03b2 oligomers and fibrils can act directly as major toxic agents and indirectly as pools of the toxic entities, respectively. Thus, the detection of A\u03b2 aggregates is of diagnostic interest and should benefit enhanced molecular understanding of AD. Among many molecular platforms, peptide-based ligands hold promise as A\u03b2 probes due to their relative simplicity, ease of optimization and facile conjugation to other molecular contexts. In this regard, A\u03b2 hydrophobic segments (critical in A\u03b2 self-assembly) or variants thereof can serve as lead molecules for A\u03b2 probe development. Unfortunately, the resulting peptides are either highly self-aggregation-prone or their probe potential has not been thoroughly examined. In the present study, we characterized a novel peptide ligand, KLVFWAK, which was created by simple point mutations of an A\u03b2 hydrophobic segment (16KLVFFAE22). We found that KLVFWAK displayed low self-aggregation propensity and was preferentially bound to A\u03b2 oligomers and fibrils relative to A\u03b2 monomers. Interestingly, binding of KLVFWAK to A\u03b2 aggregates occurred at a non-homologous A\u03b2 segment (e.g., A\u03b2 C-terminal domain) rather than the homologous 16KLVFFAE22. We also show that detection of A\u03b2 aggregates during incubation of fresh A\u03b2 was possible with KLVFWAK, further supporting KLVFWAK's high probe potential for A\u03b2 aggregates. In short, this study presents creation of a non-self-aggregating peptide ligand for A\u03b2 aggregates through simple point mutation of an A\u03b2-derived segment.<\/jats:p>\n                  <jats:p\/>","DOI":"10.1039\/c5mb00280j","type":"journal-article","created":{"date-parts":[[2015,6,4]],"date-time":"2015-06-04T12:30:23Z","timestamp":1433421023000},"page":"2281-2289","update-policy":"https:\/\/doi.org\/10.1039\/rsc_crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Engineering of a peptide probe for \u03b2-amyloid aggregates"],"prefix":"10.1093","volume":"11","author":[{"given":"Edwin","family":"Aoraha","sequence":"first","affiliation":[{"name":"Othmer-Jacobs Department of Chemical and Biomolecular Engineering, New York University a , 6 MetroTech Center, Brooklyn, NY 11201, USA \u00a0 jin.kim@nyu.edu \u00a0 +1 718-260-3125 \u00a0 +1-718-260-3719"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jason","family":"Candreva","sequence":"additional","affiliation":[{"name":"Othmer-Jacobs Department of Chemical and Biomolecular Engineering, New York University a , 6 MetroTech Center, Brooklyn, NY 11201, USA \u00a0 jin.kim@nyu.edu \u00a0 +1 718-260-3125 \u00a0 +1-718-260-3719"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jin Ryoun","family":"Kim","sequence":"additional","affiliation":[{"name":"Othmer-Jacobs Department of Chemical and Biomolecular Engineering, New York University a , 6 MetroTech Center, Brooklyn, NY 11201, USA \u00a0 jin.kim@nyu.edu \u00a0 +1 718-260-3125 \u00a0 +1-718-260-3719"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2015,6,4]]},"reference":[{"key":"2026010815121521500_cit1","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1212\/WNL.0b013e31828726f5","volume":"80","author":"Hebert","year":"2013","journal-title":"Neurology"},{"key":"2026010815121521500_cit2","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","volume":"8","author":"Haass","year":"2007","journal-title":"Nat. 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