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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Lasso peptide, a highly stable structure and designable multifunctional backbone.

Ning Zhao1, Yongxu Pan1, Zhen Cheng2

  • 1Institute of Molecular Medicine, College of Life and Health Sciences, Northeastern University, Shenyang, 110000, China.

Amino Acids
|April 15, 2016
PubMed
Summary
This summary is machine-generated.

Lasso peptides are stable natural products with potent antibacterial activity. Modifications to their structure, particularly the loop region, show promise for developing new medical applications and cancer therapies.

Keywords:
Antibacterial activityBiosynthesisLasso peptideScaffold proteinThree-dimensional structure

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Area of Science:

  • Natural Product Chemistry
  • Structural Biology
  • Medicinal Chemistry

Background:

  • Lasso peptides represent a unique class of natural products characterized by compact and stable structures.
  • These peptides exhibit diverse biological activities, with antibacterial efficacy being a primary focus.
  • Ongoing research involves discovering novel lasso peptides and elucidating their biosynthetic and chemical synthesis pathways.

Purpose of the Study:

  • To explore the structural features of lasso peptides, focusing on the ring, loop, and tail regions.
  • To understand the mechanisms underlying their antibacterial activity and identify regions suitable for modification.
  • To investigate the potential of modified lasso peptides for therapeutic applications, including cancer treatment.

Main Methods:

  • Advanced techniques for the discovery and analysis of novel lasso peptides.
  • Studies on the biosynthesis and chemical synthesis of lasso peptides.
  • Structural identification and characterization of lasso peptide components, including the loop and tail.
  • Grafting specific ligands (e.g., arginine, glycine, aspartic acid) to the lasso peptide loop.

Main Results:

  • The ring structure is crucial for the compact, stable conformation and antibacterial properties of lasso peptides.
  • The loop region (e.g., V11-S18 of MccJ25) can be modified without disrupting the overall lasso structure.
  • Grafting cancer-targeting ligands to the loop retained bioactivity, suggesting potential for targeted therapies.
  • The tail region, an immunity protein, facilitates export and self-protection.

Conclusions:

  • Lasso peptides possess inherent structural stability and potent bioactivity, making them attractive scaffolds for drug development.
  • Modification of the loop region offers a viable strategy for creating novel therapeutic agents.
  • The non-pathogenic nature of most known lasso peptides enhances their suitability for medical applications.
  • Future research should focus on multi-molecular modifications and large-scale production for multifunctional lasso peptide development.