具有 2:3 和 2:2:1 计量比的自组装蛋白-芳香折叠体复合物。
Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries.
机构信息
CBMN (UMR5248), Univ. Bordeaux, CNRS, IPB , Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33600 Pessac, France.
Department of Organic and Pharmaceutical Technology, Faculty of Chemistry, Wrocław University of Science and Technology , 50-370 Wrocław, Poland.
出版信息
J Am Chem Soc. 2017 Mar 1;139(8):2928-2931. doi: 10.1021/jacs.7b00184. Epub 2017 Feb 14.
The promotion of protein dimerization using the aggregation properties of a protein ligand was explored and shown to produce complexes with unusual stoichiometries. Helical foldamer 2 was synthesized and bound to human carbonic anhydrase (HCA) using a nanomolar active site ligand. Crystal structures show that the hydrophobicity of 2 and interactions of its side chains lead to the formation of an HCA-2 complex in which three helices of 2 are stacked, two of them being linked to an HCA molecule. The middle foldamer in the stack can be replaced by alternate sequences 3 or 5. Solution studies by CD and NMR confirm left-handedness of the helical foldamers as well as HCA dimerization.
利用蛋白质配体的聚集特性促进蛋白质二聚化的方法得到了探索，并表明可以产生具有不寻常化学计量比的复合物。合成了螺旋折叠体 2，并使用纳摩尔级的活性位点配体与人类碳酸酐酶（HCA）结合。晶体结构表明，2 的疏水性及其侧链相互作用导致形成 HCA-2 复合物，其中 2 的三条螺旋堆叠，其中两条与 HCA 分子相连。堆叠中的中间折叠体可以被交替序列 3 或 5 替换。通过 CD 和 NMR 的溶液研究证实了螺旋折叠体以及 HCA 二聚化的左手性。
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