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Discovery, Function, and Engineering of Graspetides.

Brian Choi1, A James Link1,2,3

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|August 24, 2023
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Summary
This summary is machine-generated.

Graspetides, a class of modified peptides, feature unique macrocyclic structures formed by ATP-grasp enzymes. This review explores their discovery, genomics, bioactivity, and future research directions in peptide science.

Keywords:
GraspetidesRiPPsnatural product

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Products Chemistry

Background:

  • Graspetides are ribosomally synthesized and post-translationally modified peptides (RiPPs) characterized by macrocyclic structures.
  • These structures arise from ester or amide linkages between peptide side chains, catalyzed by ATP-grasp enzymes.

Purpose of the Study:

  • To review the discovery and characterization of graspetides, including early isolations and genomics-based identification.
  • To discuss the mechanism and structure of ATP-grasp enzymes involved in graspetide biosynthesis.
  • To explore graspetide bioactivity, chemical modifications, and engineering potential.

Main Methods:

  • Activity-based isolation of initial graspetide compounds.
  • Genomics-driven approaches for identifying novel graspetides.
  • Analytical techniques for determining graspetide linkage structures.
  • Review of existing literature on graspetide bioactivity and modifications.

Main Results:

  • Established graspetides (marinostatins, microviridins) as RiPPs through key experiments.
  • Detailed understanding of ATP-grasp enzyme function in forming graspetide macrocycles.
  • Compilation of knowledge on graspetide protease inhibitory activities.
  • Overview of chemical modifications and engineering efforts.

Conclusions:

  • Graspetides represent a significant class of RiPPs with diverse bioactivities.
  • Further research into genome mining and analytical methods will uncover more graspetides.
  • Graspetide engineering holds promise for developing novel therapeutics.