Peptides articles from across Nature Portfolio

The discovery of macrocyclic peptide therapeutics has been slow. We introduce RFpeptides, a deep learning method that enables the de novo design of macrocyclic peptide binders to therapeutic targets. The designed macrocycles bind their respective protein targets with high affinity and atomic-level accuracy.

The spider Cheiracanthium punctorium evolved defensive venom rich in CSTX peptides and PLA₂ enzymes. These components arose via gene duplication, fusion, and convergence, reflecting how similar ecological pressures shape venom evolution.

Constructing synthetic mimics of membraneless organelles using small molecules can contribute towards our understanding of active phase separation and their role in the chemical emergence of compartments. Herein, the authors develop a model of synthetic membraneless organelles as non-equilibrium droplet phase which are accessed via homotypic interactions between small activated molecule and short peptides.

The biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs) involves binding of the N-terminal leader region of precursor peptides to peptide modifying enzymes and subsequent modification of the C-terminal core. Here, the authors describe the intermolecular protein-protein interactions that guide the post translational modification of atypically large and structured RiPP precursor peptides.

Nature-inspired catalysts strive to emulate the efficiency and selectivity of enzymes while maintaining the robustness of synthetic catalysts. Here, the authors use bioinformatics to design an eight-amino-acid peptide that self-assembles with copper ions, forming a complex that mimics the laccase enzyme’s active site, highlighting the potential of short peptides in biomimetic catalysis.

The discovery of macrocyclic peptide therapeutics has been slow. We introduce RFpeptides, a deep learning method that enables the de novo design of macrocyclic peptide binders to therapeutic targets. The designed macrocycles bind their respective protein targets with high affinity and atomic-level accuracy.

A deep-learning framework identifies peptides that show antimicrobial activity against multidrug-resistant bacteria, eradicate biofilms, and treat intestinal bacterial infection in mice.

Transposition is normally considered a DNA-based process. Now, scientists have devised a means to carry out a similar transformation — this time using proteins. The approach enables protein semisynthesis and site-specific modification of folded substrates in vitro and in live cells, opening up new ways to probe and manipulate biological systems.

In 1961, it was demonstrated that the enzyme ribonuclease can correctly fold upon oxidation in air from a fully reduced and denatured polypeptide chain. Since then, the principles that govern the oxidative folding of polypeptide chains have been elucidated, and our ability to control this process has advanced significantly.