Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS), Departamento de Química Orgánica, Universidade de Santiago de Compostela, 15782 Santiago de Compostela, Spain.
Chem Commun (Camb). 2018 Jun 19;54(50):6919-6922. doi: 10.1039/c8cc02304b.
Even for short peptides that are enriched in basic amino acids, the large chemical space that can be spanned by combinations of natural amino acids hinders the rational design of cell penetrating peptides. We here report on short oligoalanine scaffolds for the fine-tuning of peptide helicity in different media and the study of cell penetrating properties. This strategy allowed the extraction of the structure/activity features required for maximal membrane interaction and cellular penetration at minimal toxicity. These results confirmed oligoalanine helical callipers as optimal scaffolds for the rational design and the identification of cell penetrating peptides.
即使对于富含碱性氨基酸的短肽，天然氨基酸组合可以跨越的巨大化学空间也阻碍了细胞穿透肽的合理设计。在这里，我们报告了短的寡丙氨酸支架，用于在不同介质中微调肽的螺旋性，并研究细胞穿透特性。该策略允许提取最大膜相互作用和最小毒性所需的结构/活性特征。这些结果证实了寡丙氨酸螺旋卡尺是合理设计和鉴定细胞穿透肽的最佳支架。
