Official Project Description
Graspetides are a class of ribosomally synthesized and post-translationally modified peptides (RiPPs) characterized by the ATP-grasp ligase–catalyzed macrolactam or macrolactone linkages in their structure.
These macrocycles impart structural stability and diverse bioactivities, including antimicrobial, antiviral, and enzyme inhibitory effects.
Graspetides are classified into distinct groups based on sequence motifs, cyclization patterns, and biosynthetic machinery.
While each group exhibits characteristic ring topologies, the molecular basis by which core peptide sequence and folding pathways dictate the order of ring formation remains poorly understood. In this study, we will investigate the interactions between graspetide precursor peptides and their respective ATP-grasp ligases using atomic-level molecular dynamics (MD) simulations.
By comparing the folding trajectories of these systems under differing conditions, we aim to identify and assess patterns in ring closure preference.