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H-1, C-13 and N-15 assignments of a camelid nanobody directed against human alpha-synuclein

Vuchelen, A; O'Day, E; De Genst, E; Pardon, E; Wyns, L; Dumoulin, M; Dobson, CM; ... Hsu, STD; + view all (2009) H-1, C-13 and N-15 assignments of a camelid nanobody directed against human alpha-synuclein. BIOMOL NMR ASSIGN , 3 (2) 231 - 233. 10.1007/s12104-009-9182-4.

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Abstract

Nanobodies are single chain antibodies that are uniquely produced in Camelidae, e.g. camels and llamas. They have the desirable features of small sizes (Mw < 14 kDa) and high affinities against antigens (Kd similar to nM), making them ideal as structural probes for biomedically relevant motifs both in vitro and in vivo. We have previously shown that nanobody binding to amyloidogenic human lysozyme variants can effectively inhibit their aggregation, the process that is at the origin of systemic amyloid disease. Here we report the NMR assignments of a new nanobody, termed NbSyn2, which recognises the C-terminus of the intrinsically disordered protein, human alpha-synuclein (aS), whose aberrant self-association is implicated in Parkinson's disease.

Type: Article
Title: H-1, C-13 and N-15 assignments of a camelid nanobody directed against human alpha-synuclein
DOI: 10.1007/s12104-009-9182-4
Keywords: Camelid antibody, Nanobody, Alpha-synuclein, Intrinsically disordered protein, Parkinson's disease, ANTIBODY FRAGMENT, AMYLOID FIBRILS, HUMAN LYSOZYME, LLAMA
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1318773
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