RiPPing apart the rules for peptide natural products

作     者：Aman S.Imani Michael F.Freeman 

作者机构：Department of BiochemistryMolecular Biologyand Biophysics&BioTechnology InstituteUniversity of Minnesota-Twin CitiesSt.PaulMN 55108USA 

出 版 物：《Synthetic and Systems Biotechnology》 (合成和系统生物技术（英文）)

年 卷 期：2018年第3卷第2期

页      面：81-82页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：University of Minnesota BioTechnology Institute 

主　　题：synthesis. canonical backbone 

摘      要：Humankind has looked to peptide natural products as a source of valuable therapeutics harboring anti-cancer,immunomodulatory,and antibiotic properties since the discovery of penicillin in the late *** natural products display a wide array of proteolytically resistant backbone modifications,non-canonical amino acids,and cyclizations that rigidify their structures and enable binding to specific cellular *** distinct biosynthetic routes yield nearly all complex modified peptides currently identifieddthose incorporating amino acids via the ribosome and those that use multimodular protein complexes,termed non-ribosomal peptide synthetases(NRPSs),to ligate individual amino acids in an assembly-line *** ribosomal synthesis,NRPSderived peptides are not limited to the canonical 20 amino *** have been shown to incorporate upwards of 500 unique amino acids directly into their peptide scaffolds[1].The impressive amino acid building block repertoire of NRPS-derived peptides was thought to cover a much larger structural and chemical space compared to their ribosomally-derived *** ribosomally synthesized and post-translationally modified peptide(RiPP)pathways are currently known to introduce unique lanthionine thioether linkages and lasso peptide-like topologies[2]compared to NRPS pathways,for many years these examples were minor concessions to the breadth of distinct modifications only thought possible for non-ribosomal *** the(RiPP)tides are turning,and in dramatic fashion.