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首页> 外文期刊>Biomolecular NMR assignments >p#H, p#pdC and p#eN assignments of a camelid nanobody directed against human l-synuclein
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p#H, p#pdC and p#eN assignments of a camelid nanobody directed against human l-synuclein

机译:针对人l-突触核蛋白的骆驼科纳米粒的p#H,p#pdC和p#eN分配

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摘要

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.
机译:纳米抗体是在骆驼科(Camelidae)中独特产生的单链抗体,例如。骆驼和美洲驼。它们具有小尺寸(Mw <14 kDa)和对抗原的高亲和力(Kd大约nM)的理想特性,使其非常适合作为体内外生物医学相关基序的结构探针。先前我们已经表明,与产生淀粉样蛋白的人类溶菌酶变异体结合的纳米抗体可以有效抑制其聚集,而这一过程是系统性淀粉样蛋白疾病的起源。在这里,我们报告了一个新的称为NbSyn2的纳米抗体的NMR指配,该抗体识别内在无序的蛋白质人类α-突触核蛋白(aS)的C末端,其异常的自缔合与帕金森氏病有关。

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