School of Chemistry and ‡School of Biochemistry, University of Bristol , Bristol BS8 1TS, United Kingdom.
J Am Chem Soc. 2013 Apr 3;135(13):5161-6. doi: 10.1021/ja312310g. Epub 2013 Mar 19.
The availability of peptide and protein components that fold to defined structures with tailored stabilities would facilitate rational protein engineering and synthetic biology. We have begun to generate a toolkit of such components based on de novo designed coiled-coil peptides that mediate protein-protein interactions. Here, we present a set of coiled-coil heterodimers to add to the toolkit. The lengths of the coiled-coil regions are 21, 24, or 28 residues, which deliver dissociation constants in the micromolar to sub-nanomolar range. In addition, comparison of two related series of peptides highlights the need for including polar residues within the hydrophobic interfaces, both to specify the dimer state over alternatives and to fine-tune the dissociation constants.
具有特定稳定性的折叠成定义结构的肽和蛋白质成分的可用性将促进理性的蛋白质工程和合成生物学。我们已经开始基于介导蛋白质-蛋白质相互作用的从头设计的卷曲螺旋肽来生成此类组件的工具包。在这里，我们提出了一组卷曲螺旋异二聚体以添加到工具包中。卷曲螺旋区的长度为 21、24 或 28 个残基，其解离常数在微摩尔到亚纳摩尔范围内。此外，对两个相关系列肽的比较突出表明需要在疏水区内包含极性残基，这既是为了指定二聚体状态而不是其他状态，也是为了微调解离常数。
