针对人α-突触核蛋白的骆驼科纳米抗体的（1）H、（13）C和（15）N归属
(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.
作者信息
Vuchelen Anneleen, O'Day Elizabeth, De Genst Erwin, Pardon Els, Wyns Lode, Dumoulin Mireille, Dobson Christopher M, Christodoulou John, Hsu Shang-Te Danny
机构信息
Department of Chemistry, University of Cambridge, Cambridge, UK.
出版信息
Biomol NMR Assign. 2009 Dec;3(2):231-3. doi: 10.1007/s12104-009-9182-4.
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 approximately 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.
纳米抗体是仅在骆驼科动物（如骆驼和羊驼）中产生的单链抗体。它们具有尺寸小（分子量<14 kDa）和对抗原亲和力高（解离常数约为纳摩尔）的理想特性，使其成为体内外生物医学相关基序的理想结构探针。我们之前已经表明，纳米抗体与淀粉样生成的人溶菌酶变体结合可以有效抑制其聚集，而聚集过程是全身性淀粉样疾病的根源。在此，我们报告了一种名为NbSyn2的新纳米抗体的核磁共振（NMR）归属，该纳米抗体识别内在无序蛋白人α-突触核蛋白（αS）的C端，其异常的自我缔合与帕金森病有关。
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