RESEARCH: CANCER
FOLDING PROJECT #15309 PROFILE

This project investigates how different types of graspetides, small proteins with unique rings, fold into their shapes. By using computer simulations, researchers will explore the order in which these rings form and try to understand what makes each type of graspetide unique.

Note: This TLDR is a simplication and may not be 100% accurate.

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 model species from multiple graspetide groups using atomic-level molecular dynamics (MD) simulations.

By comparing folding trajectories across these representative systems, we aim to identify conserved and group-specific determinants of ring pattern formation, and to assess whether distinct biosynthetic groups exhibit preferences for particular ring closure orders.

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Graspetides

A class of ribosomally synthesized and post-translationally modified peptides (RiPPs).

Graspetides are a type of peptide produced by living organisms. They have unique structures with rings called macrolactam or macrolactone linkages. These rings make them strong and give them various abilities, such as fighting bacteria and viruses. Scientists are studying how graspetides form these rings and what makes different types unique.

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Ribosomally synthesized and post-translationally modified peptides (RiPPs)

Ribosomally synthesized and post-translationally modified peptides (RiPPs)

RiPPs are a special type of peptide made by ribosomes (the protein factories in cells). After being made by ribosomes, RiPPs go through changes that make them more complex and useful. They have many important functions in living things.

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Macrolactam

A cyclic amide formed by the reaction of an amine with a carboxylic acid.

Macrolactam is a type of ring structure found in some peptides. It's formed when a part of the peptide chain connects back to itself through a chemical bond. This makes the peptide more stable and can give it special properties.

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Macrolactone

A cyclic ester formed by the reaction of a carboxylic acid with an alcohol.

Macrolactone is another type of ring structure found in some peptides. It's formed when a part of the peptide chain connects back to itself through a different chemical bond. Like macrolactam, it makes the peptide more stable and can give it special properties.

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Molecular dynamics (MD)

Molecular dynamics (MD)

Molecular dynamics is a computer simulation technique used to study how atoms and molecules move and interact over time. It's a powerful tool for understanding the behavior of complex systems like proteins and DNA.