ATP selection in a random peptide library consisting of prebiotic amino acids

作者：Kang, Shou-Kai; Chen, Bai-Xue; Tian, Tian; Jia, Xi-Shuai; Chu, Xin-Yi; Liu, Rong; Dong, Peng-Fei; Yang, Qing-Yong; Zhang, Hong-Yu^*

来源：Biochemical and Biophysical Research Communications, 2015, 466(3): 400-405.

DOI：10.1016/j.bbrc.2015.09.038

• Origin of proteins
• Protein evolution
• Structure and function
• cDNA display
• In vitro selection
• Next-generation sequencing

Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well.

• 出版日期2015-10-23
• 单位华中农业大学