Kazim A L, Atassi M Z
Biochem J. 1980 Jun 1;187(3):661-6. doi: 10.1042/bj1870661.
By applying the concept of 'surface-simulation' synthesis to the combining site of the myeloma protein M-603 we were able to mimic synthetically its phosphorylcholine-binding characteristics. The synthetic surface-simulation peptide was found to bind to phosphorylcholine, whereas a control peptide that had the same amino acid composition but a different sequence showed little or no binding activity. The specificity of the binding was further confirmed by inhibition studies in which the surface-simulation peptide, but not the control peptide, inhibited the binding of 125I-labelled surface-simulation peptide to phosphorylcholine. Furthermore, the surface-simulation peptide was found to completely inhibit the binding of the native myeloma protein, M-603, to phosphorylcholine. The control peptide was unable to inhibit this binding. These findings suggest that surface-simulation synthesis can be effectively employed to mimic synthetically antibody combining sites, and may in the future be a valuable tool with which to manipulate the immune response to clinically important antigens.
通过将“表面模拟”合成概念应用于骨髓瘤蛋白M - 603的结合位点,我们能够合成模拟其磷酸胆碱结合特性。发现合成的表面模拟肽能与磷酸胆碱结合,而具有相同氨基酸组成但序列不同的对照肽显示出很少或没有结合活性。结合的特异性通过抑制研究进一步得到证实,在该研究中,表面模拟肽而非对照肽抑制了125I标记的表面模拟肽与磷酸胆碱的结合。此外,发现表面模拟肽能完全抑制天然骨髓瘤蛋白M - 603与磷酸胆碱的结合。对照肽无法抑制这种结合。这些发现表明表面模拟合成可有效地用于合成模拟抗体结合位点,并且在未来可能成为一种有价值的工具,用于调控对临床重要抗原的免疫反应。