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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Updated: Jul 3, 2025

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
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Sequence-function mapping of proline-rich antimicrobial peptides.

Jonathan Collins1, Adam McConnell1, Zachary D Schmitz2

  • 1Biomedical Engineering, Minneapolis, MN 55455.

Biorxiv : the Preprint Server for Biology
|February 14, 2024
PubMed
Summary
This summary is machine-generated.

Antimicrobial peptides (AMPs) show improved function through sequence-activity mapping. This high-throughput technique reveals key mutations for enhanced potency and specificity in antibiotic drug discovery.

Keywords:
SAMP-Depantimicrobial peptidesapidaceinmetalnikowinsequence-function mapping

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Area of Science:

  • Biochemistry and Molecular Biology
  • Microbiology
  • Drug Discovery

Background:

  • Antimicrobial peptides (AMPs) are crucial for innate immunity and potential therapeutics.
  • Designing effective AMPs is challenging due to complex structure-activity relationships.
  • Existing methods for AMP discovery are limited in throughput and scope.

Approach:

  • Applied sequence-activity mapping of AMPs via depletion (SAMP-Dep), a high-throughput technique.
  • Analyzed proline-rich AMPs, metalnikowin 1 (Met) and apidaecin 1b (Api), characterizing thousands of mutants.
  • Validated SAMP-Dep reproducibility and mapped sequence-activity relationships for Met and Api.

Key Points:

  • Identified distinct mutational profiles and tolerance at proline sites within AMPs.
  • Revealed beneficial mutations at specific termini (C-terminus for Met, N-terminus for Api).
  • Observed significant epistasis within the peptide segments interacting with the ribosomal exit tunnel.

Conclusions:

  • SAMP-Dep provides robust, high-throughput characterization of AMP sequence-activity space.
  • Generated AMP variants with enhanced potency and specificity against Gram-negative bacteria.
  • Demonstrated the platform's utility for fundamental insight and therapeutic engineering of AMPs.