【摘要】 核磁共振饱和转移差谱（STD-NMR）技术能够用于检测小分子配基与大分子蛋白之间的亲和性。利用STD-NMR技术评价了基于Protein A设计的仿生肽段与人抗体（hIgG）的亲和力以及结合机制,从中筛选出了与抗体亲和性最强的仿生六肽FYEILH,利用静态吸附试验确定了此六肽与抗体的亲和力（K_d）为0.8×10^-6 mol/L,静态结合载量为61.22 mg/mL,与目前文献中报道的许多多肽配基相比,具有明显的优势。在本研究中成功将Protein A最小化,获得了与抗体具有高亲和性的Protein A仿生多肽配基。更多还原

【Abstract】 Saturation transfer difference NMR（STD-NMR）technique could be used to detect the affinity between small molecule ligands and macromolecular proteins.Here STD-NMR technique was used to evaluate the affinity and binding mechanism of biomimetic peptides and hIgG by minimizing the Protein A.A short hexapeptide（FYEILH） was thus obtained. The binding capacity of the hexapeptide was studied by static adsorption experiment.The hexapeptide presented a comparable binding activity with other peptides in the literatures,with the dissociation constant（K_d） of 0.8×10^-6 mol/L,the static binding capacity of 61.22 mg/mL.A smaller functional peptide ligand with high affinity to the antibody was obtained by reducing larger binding domains of huge Protein A molecule.更多还原