Gu-ONNRPVYIPRPRPPHPRL-OH (Gu = N,N,N’,N’-tetramethylGuanidino and O = L-ornithine)
长度 (aa)
18
多肽纯度 (HPLC)
97.0
分子式
C104H171N37O22
分子量
2291.40
来源
固相合成
其他信息
Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination.
Florin T, Maracci C, Graf M, et al. An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Nat Struct Mol Biol. 2017
bioRxiv preprint doi: https://doi.org/10.1101/2020.05.17.100735. this version posted May 20, 2020.
Mardirossian M, Barrière Q, Timchenko T, et al. Fragments of the Nonlytic Proline-Rich Antimicrobial Peptide Bac5 Kill Escherichia coli Cells by Inhibiting Protein Synthesis. Antimicrob Agents Chemother. 2018;62(8):e00534-18. Published 2018 Jul 27. doi:10.1128/AAC.00534-18
Meydan S, Marks J, Klepacki D, et al. Retapamulin-Assisted Ribosome Profiling Reveals the Alternative Bacterial Proteome. Mol Cell. 2019;74(3):481-493.e6
Adio S, Sharma H, Senyushkina T, et al. Dynamics of ribosomes and release factors during translation termination in E. coli. Elife. 2018
Florin T, Maracci C, Graf M, et al. An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Nat Struct Mol Biol. 2017;24(9):752-757