Peptides were designed to inhibit the protein–protein interaction of CD2 and CD58 to modulate the immune response. This work involved the design and synthesis of eight different peptides by replacing each amino acid residue in peptide 6 with alanine as well as grafting the peptide to the sunflower trypsin‐inhibitor framework. From the alanine scanning studies, mutation at position 2 of the peptide was shown to result in increased potency to inhibit cell adhesion interactions. The most potent peptide from the alanine scanning was further studied for its detailed three‐dimensional structure and binding to CD58 protein using surface plasmon resonance and flow cytometry. This peptide was used to graft to the sunflower trypsin inhibitor to improve the stability of the peptide. The grafted peptide, SFTI‐a1, was further studied for its potency as well as its thermal, chemical, and enzymatic stability. The grafted peptide exhibited improved activity compared to our previously grafted peptide and was stable against thermal and enzymatic degradation.

中文翻译：

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通过移植肽调节来自 CD2-CD58 蛋白的共刺激信号

肽旨在抑制 CD2 和 CD58 的蛋白质-蛋白质相互作用以调节免疫反应。这项工作涉及通过替换肽6中的每个氨基酸残基来设计和合成八种不同的肽与丙氨酸以及将肽接枝到向日葵胰蛋白酶抑制剂框架上。丙氨酸扫描研究表明，肽的第 2 位突变导致抑制细胞粘附相互作用的效力增加。使用表面等离子共振和流式细胞术进一步研究了丙氨酸扫描中最有效的肽的详细三维结构和与 CD58 蛋白的结合。该肽用于嫁接向日葵胰蛋白酶抑制剂，以提高肽的稳定性。进一步研究了接枝肽 SFTI-a1 的效力以及热稳定性、化学稳定性和酶稳定性。与我们之前的接枝肽相比，接枝肽表现出更高的活性，并且对热降解和酶降解稳定。