Plant-derived ring peptides inspire precise new drug designs
Zhou Y, Li N, Zheng JS
Medicinal Plants
The tough, ring-shaped proteins some plants make as a defense against pests, called cyclotides, turn out to be so stable and precisely shaped that drug designers are now studying them as blueprints for new medicines.
Some plants make small looped proteins called cyclotides that are unusually tough and hold their shape well, originally as a defense against insects and other threats. Researchers are now looking at these plant molecules, alongside similar ring-shaped peptides from venom and microbes, to design new drugs that fit snugly into specific cell receptors involved in things like pain, appetite, and hormone signaling. The plant compounds serve as natural templates that chemists can tweak and improve in the lab.
Key Findings
Review covers four natural sources of cyclic peptide drug templates: endogenous human peptides, venom-derived peptides, plant cyclotides, and microbial macrocycles
Engineering strategies discussed include bridge replacement, conformational locking, residue modification, and half-life extension to improve these molecules as drug candidates
Discovery technologies highlighted include mRNA display, phage display, cell-based screening, and computational structure-guided design for finding new GPCR-targeting macrocycles
chevron_right Technical Summary
Scientists are studying ring-shaped peptides, some borrowed from plants, venoms, and microbes, as a new way to design drugs that lock onto specific hormone receptors in the body more precisely than typical pills can.
Abstract Preview
Original paper
Advances in Cyclic Peptides Targeting G Protein-Coupled Receptors.
Peptide-responsive G protein-coupled receptors (GPCRs) often recognize endogenous peptide ligands through extended receptor interfaces, providing opportunities for peptide-based ligands to engage r...
open_in_new Read full abstractAbstract copyright held by the original publisher.
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In biochemistry, cyclotides are small, disulfide-rich peptides isolated from plants. Typically containing 28–37 amino acids, they are characterized by their head-to-tail cyclised peptide backbone and the interlocking arrangement of their three disulfide bonds. These combined features have been te...