A review published in The Journal of Antibiotics on 26 October 2026 examines how the biosynthetic machinery of ribosomally synthesized and post-translationally modified peptides, known as RiPPs, can be harnessed to decorate artificial peptides with post-translational modifications. Written by Shinta Ijichi, Shumpei Asamizu, Shotaro Hoshino and Hiroyasu Onaka, the review gathers recent bioengineering approaches in which RiPP modification enzymes act on substrates that diverge substantially from their natural targets, including large combinatorial peptide libraries, de novo designed peptides and chemically synthesized peptides. Post-translational modifications are enzymatic conversions that alter peptides after they are translated, and the review describes them as a promising route for introducing desired chemical and biological properties into peptide molecules.
Nature relies heavily on this strategy: many bioactive peptidic natural products acquire their unique structures and functions through diverse enzymatic transformations. RiPPs are highlighted as a prominent example and constitute a major group of peptidic natural products generated through various post-translational modifications of ribosomally translated precursor peptides. According to the authors, the biosynthetic features of RiPPs make their modification enzymes a valuable foundation for peptide bioengineering.
Because these enzymes normally operate on ribosomally produced precursor peptides, researchers have developed numerous engineering approaches to redirect them toward artificial substrates. The review documents how this capability has progressively expanded beyond native RiPP substrates to artificial peptides that differ considerably from the sequences these enzymes encounter in their producing organisms. The reviewed approaches span three categories of artificial peptides: large combinatorial peptide libraries, de novo designed peptides and chemically synthesized peptides.
In each case, RiPP post-translational modification enzymes serve as the catalytic tools that install modifications onto these non-native substrates, extending the reach of the enzymes well past the precursor peptides they modify in nature. The review concludes that these advances demonstrate the potential of RiPP biosynthetic machinery as a versatile toolkit for expanding peptide chemical space and for generating bioactive artificial peptides. As a review article, it synthesizes and evaluates previously published work rather than reporting new experimental findings, and the authors note that no datasets were generated or analysed during the study.
Subject of Research: Enzymatic installation of post-translational modifications into artificial peptides using RiPP biosynthetic machinery
Article Title: Enzymatic installation of post-translational modifications into artificial peptides using RiPP biosynthetic machinery
Article References: Ijichi, S., Asamizu, S., Hoshino, S., & Onaka, H. (2026). Enzymatic installation of post-translational modifications into artificial peptides using RiPP biosynthetic machinery. The Journal of Antibiotics. https://doi.org/10.1038/s41429-026-00964-6
Image Credits: AI Generated
DOI: 10.1038/s41429-026-00964-6
Keywords: Enzymatic, installation, post-translational, modifications, artificial, peptides, RiPP, biosynthetic, machinery, scientific research
News Source: Ophelia Keating. (October 26, 2026). Enzymatic installation of post-translational modifications into artificial peptides using RiPP biosynthetic machinery. Scienmag.
