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Related Concept Videos

Antimicrobial Proteins01:23

Antimicrobial Proteins

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Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
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Macrocyclic Antimicrobial Peptides Engineered from ω-Conotoxin.

Xinya Hemu1, James P Tam1

  • 1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 03s-71, Singapore 637551, Singapore.

Current Pharmaceutical Design
|March 2, 2017
PubMed
Summary
This summary is machine-generated.

Macrocyclization transforms a conotoxin into a potent antimicrobial peptide. Modifications improved activity against bacteria and enhanced immune cell attraction, offering new therapeutic design strategies.

Keywords:
Macrocyclizationantimicrobial peptidechemotaxis.cyclic conotoxin

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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Peptide Science

Background:

  • Omega-conotoxin MVIIA is a linear peptide known for blocking calcium channels.
  • It possesses multiple basic amino acids at its termini.
  • Its structure is characterized by a cystine-knot motif.

Purpose of the Study:

  • To investigate the antimicrobial potential of macrocyclized conotoxin MVIIA analogs.
  • To evaluate the impact of disulfide bond conversion to amino butyric acids on activity.
  • To assess the chemotactic activity of modified analogs against human monocytes.

Main Methods:

  • Preparation of ten macrocyclic analogs using Boc and Fmoc chemistry via native chemical ligation.
  • Testing antimicrobial activity against Gram-positive and Gram-negative bacteria.
  • Assessing chemotactic activity using human monocyte THP-1 cells.
  • Evaluating molecular stability against thermal and acid treatments.

Main Results:

  • All cyclic analogs exhibited antimicrobial activity in the low micromolar range, unlike the inactive parent peptide.
  • Conversion of disulfide bonds to amino butyric acids enhanced antimicrobial efficacy.
  • Cyclic analogs demonstrated 2-3 fold improved chemotactic activity compared to MVIIA.
  • Backbone cyclization partially restored molecular stability lost by reducing disulfide bonds.

Conclusions:

  • Macrocyclization and side chain modification of conopeptides can lead to novel antimicrobial peptides.
  • These modifications result in a gain-of-function, converting a calcium channel blocker into an antimicrobial agent.
  • This approach offers a new perspective for designing and engineering peptidyl therapeutics.