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10.1038/s41598-017-06377-8 http://scihub22266oqcxt.onion/10.1038/s41598-017-06377-8 C5519597!5519597!28729665     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28729665&cmd=llinks): Failed to open stream: HTTP request failed! 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Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid-? |pdf=|usr=}}{{28729665}} gab.com Text Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid- JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28729665 #FOAvip Protofibrils of the 42 amino acids long amyloid-? peptide are transient pre-fibrillar intermediates in the process of peptide aggregation into amyloid plaques and are thought to play a critical role in the pathology of Alzheimer?s disease. Hence, there is a need for research reagents and potential diagnostic reagents for detection and imaging of such aggregates. Here we describe an in vitro selection of Affibody molecules that bind to protofibrils of A?42cc, which is a stable engineered mimic of wild type A?42 protofibrils. Several binders were identified that bind A?42cc protofibrils with low nanomolar affinities, and which also recognize wild type A?42 protofibrils. Dimeric head-to-tail fusion proteins with subnanomolar binding affinities, and very slow dissociation off-rates, were also constructed. A mapping of the chemical properties of the side chains onto the Affibody scaffold surface reveals three distinct adjacent surface areas of positively charged surface, nonpolar surface and a polar surface, which presumably match a corresponding surface epitope on the protofibrils. The results demonstrate that the engineered A?42cc is a suitable antigen for directed evolution of affinity reagents with specificity for wild type A?42 protofibrils. Twit Text FOAVip Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid- ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28729665 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28729665 #FOAvip English Wikipedia <ref>{{Cite pmid|28729665}}</ref> Identification of proteins that specifically recognize and bind protofibrillar aggregates of amyloid-? #MMPMID28729665 Wahlberg E; Rahman MM; Lindberg H; Gunneriusson E; Schmuck B; Lendel C; Sandgren M; Löfblom J; Ståhl S; Härd T Sci Rep 2017[]; 7 (ä): ä PMID28729665show ga Protofibrils of the 42 amino acids long amyloid-? peptide are transient pre-fibrillar intermediates in the process of peptide aggregation into amyloid plaques and are thought to play a critical role in the pathology of Alzheimer?s disease. Hence, there is a need for research reagents and potential diagnostic reagents for detection and imaging of such aggregates. Here we describe an in vitro selection of Affibody molecules that bind to protofibrils of A?42cc, which is a stable engineered mimic of wild type A?42 protofibrils. Several binders were identified that bind A?42cc protofibrils with low nanomolar affinities, and which also recognize wild type A?42 protofibrils. Dimeric head-to-tail fusion proteins with subnanomolar binding affinities, and very slow dissociation off-rates, were also constructed. A mapping of the chemical properties of the side chains onto the Affibody scaffold surface reveals three distinct adjacent surface areas of positively charged surface, nonpolar surface and a polar surface, which presumably match a corresponding surface epitope on the protofibrils. The results demonstrate that the engineered A?42cc is a suitable antigen for directed evolution of affinity reagents with specificity for wild type A?42 protofibrils. äIdentification of proteins that specifically recognize and bind protof(epmc).pdf DeepDyve Pubget Overpricing