Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Lentivirus-derived antimicrobial peptides: increased potency by sequence engineering and dimerization.

S B Tencza1, D J Creighton, T Yuan

  • 1Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, PA 15261, USA.

The Journal of Antimicrobial Chemotherapy
|August 25, 1999
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[EIAV (equine infectious anemia virus): to better understand the lentiviral pathogenesis].

Virologie (Montrouge, France)·2021
Same author

Enhanced therapeutic index of an antimicrobial peptide in mice by increasing safety and activity against multidrug-resistant bacteria.

Science advances·2020
Same author

[An efficacy and safety study of bifidobacterium tetragenous viable bacteria tablets in the treatment of constipation in patients with type 2 diabetes mellitus].

Zhonghua nei ke za zhi·2018
Same author

Measurement of Atmospheric Neutrino Oscillations at 6-56 GeV with IceCube DeepCore.

Physical review letters·2018
Same author

[Ibrutinib inhibits mesenchymal stem cells-mediated drug resistance in diffuse large B-cell lymphoma].

Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi·2018
Same author

[The clinical value of soluble urokinase plasminogen activation receptor in febrile neutropenic patients with hematological malignancies after chemotherapy].

Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi·2018

Researchers engineered antimicrobial peptides (AMPs) derived from lentivirus envelope proteins. Optimizing peptide structure, including dimerization, significantly enhanced antimicrobial potency and selectivity, leading to new therapeutic candidates.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Peptide Chemistry

Background:

  • Cationic amphipathic peptides derived from lentivirus envelope proteins exhibit antimicrobial properties.
  • Naturally occurring antimicrobial peptides (AMPs) are crucial in innate immunity.

Purpose of the Study:

  • To explore amino acid modifications (truncations, substitutions) to enhance antimicrobial potency and selectivity of the lentivirus-derived peptide LLP1.
  • To investigate the impact of disulfide-linked dimerization on antimicrobial activity.
  • To engineer a highly potent and selective antimicrobial peptide.

Main Methods:

  • Systematic amino acid truncations and substitutions of the prototype peptide LLP1.
  • Assessment of antimicrobial potency against Gram-positive and Gram-negative bacteria.

Related Experiment Videos

  • Evaluation of hemolytic activity against eukaryotic cells.
  • Disulfide bond formation to create peptide dimers.
  • Secondary structure analysis using alpha-helical content measurements.
  • Application of dimerization strategy to magainin 2.

    • Main Results:

    • C-terminal truncation of LLP1 reduced hemolytic activity without significantly affecting antimicrobial potency.
    • Substitution of glutamic acid with arginine residues increased bactericidal activity.
    • Cysteine-containing peptides spontaneously formed disulfide-linked dimers, exhibiting a 16-fold increase in bactericidal activity against Staphylococcus aureus.
    • Dimerization did not alter the secondary structure (alpha-helical content) of the peptides.
    • Dimerization of magainin 2 enhanced its bactericidal activity eight-fold.
    • The optimized peptide TL-1 demonstrated significantly improved potency against Gram-positive bacteria, maintained activity against Gram-negative bacteria, and showed low eukaryotic cell toxicity.

    Conclusions:

    • Amino acid modifications and disulfide-linked dimerization are effective strategies for enhancing antimicrobial peptide potency and selectivity.
    • The engineered peptide TL-1 represents a promising candidate for antimicrobial applications.
    • These findings provide a basis for further peptide engineering efforts in antimicrobial drug discovery.