CAS Key Laboratory of Biological Effects of Nanomaterials and Nanosafety, CAS Key Laboratory of Standardization and Measurement for Nanotechnology of Nanomaterials and Nanosafety, CAS Center for Excellence in Nanoscience, CAS Center for Excellence in Brain Science, National Center for Nanoscience and Technology, Beijing, China.
Sino-Danish Center for Education and Research, University of Chinese Academy of Sciences, Beijing, China.
J Pept Sci. 2020 Sep;26(9):e3273. doi: 10.1002/psc.3273. Epub 2020 Jun 24.
We demonstrate in this contribution the evidence that significant cooperative binding effect can be identified for the amino acid sites that are determinant to the binding characteristics in peptide-peptide interactions. The analysis of tryptophan-scanning mutagenesis of the 14-mer peptide consisting only of glycine provides a mapping of position-dependent contributions to the binding energy. The pronounced tryptophan-associated peptide-peptide interactions are originated from the indole moieties with the main chains of 14-mer glycines containing N-H and CO moieties. Specifically, with the presence of two tryptophans as determinant amino acids, cooperative binding can be observed, which are dependent on relative positions of the two tryptophans with a "volcano"-like characteristics. An optimal separation of 6-10 amino acids between two adjacent binding sites can be identified to achieve maximal binding interactions.
在本研究中，我们证明了在决定肽-肽相互作用结合特性的氨基酸位点上，可以识别出显著的协同结合效应。对仅由甘氨酸组成的 14 肽的色氨酸扫描诱变分析提供了对结合能的位置相关贡献的映射。明显的色氨酸相关的肽-肽相互作用来源于吲哚部分，其中 14 个甘氨酸的主链含有 N-H 和 C=O 部分。具体来说，有两个色氨酸作为决定氨基酸存在时，可以观察到协同结合，这种结合依赖于两个色氨酸的相对位置，具有“火山”样特征。可以确定两个相邻结合位点之间最佳的 6-10 个氨基酸的分离，以实现最大的结合相互作用。
