The chemistry of irreversible capture.
The chemistry of irreversible capture.
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DOI：
10.1016/j.addr.2008.04.010
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发表时间：
2008-09
影响因子：
16.1
通讯作者：
C. Meares
中科院分区：
文献类型：
--
作者：
C. Meares
抗体对生物分子的特异性识别和结合从根本上说是重要的。天然抗体是多价的，至少有两个相同的配体结合部位；这使得它们能够紧密结合在细胞表面，细胞表面呈现其目标配体的多个副本。与可溶性单价配体结合的抗体，如大多数小分子，不具有这种多价优势。抗体的工程片段，如单链抗体蛋白或Fab片段，也不存在，它们通常只有一个配体结合部位。工程单价抗体/配体对保留了抗体的结合特异性，但不会解离，是新的递送系统的有前途的组成部分。这些都是基于蛋白质的遗传操作和适当配体的化学合成的组合，这里回顾了这些例子。
The specific recognition and binding of biological molecules by antibodies is fundamentally important. Natural antibodies are multivalent, having at least two identical ligand-binding sites; this permits them to bind tightly at cell surfaces, which present multiple copies of their target ligands. Antibodies that bind to soluble monovalent ligands, such as most small molecules, do not share this multivalent advantage. Nor do engineered fragments of antibodies, such as single-chain Fv proteins or Fab fragments, which generally possess only a single ligand-binding site. Engineered monovalent antibody/ligand pairs that retain the binding specificity of the antibody, but do not dissociate, are promising components of new delivery systems. These are based on a combination of genetic manipulation of the protein and chemical synthesis of appropriate ligands, examples of which are reviewed here.