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 Concept Videos

Antimicrobial Proteins01:23

Antimicrobial Proteins

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...

You might also read

Related Articles

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

Sort by
Same author

Mycobacterium ulcerans ecovar infection in wild Kemp's ridley Lepidochelys kempii and loggerhead Caretta caretta sea turtles.

Diseases of aquatic organisms·2025
Same author

Effect of laminin environments and tumor factors on the biology of myeloid dendritic cells.

Immunobiology·2019
Same author

The host-defense peptide piscidin P1 reorganizes lipid domains in membranes and decreases activation energies in mechanosensitive ion channels.

The Journal of biological chemistry·2019
Same author

Structure and Function in Antimicrobial Piscidins: Histidine Position, Directionality of Membrane Insertion, and pH-Dependent Permeabilization.

Journal of the American Chemical Society·2019
Same author

Modulation of double-stranded RNA pattern recognition receptor signaling in ovarian cancer cells promotes inflammatory queues.

Oncotarget·2019
Same author

Regulation of inflammatory factors by double-stranded RNA receptors in breast cancer cells.

Immunobiology·2018

Related Experiment Video

Updated: Jul 5, 2026

Production and Testing of Antimicrobial Peptides and Their Mimics
10:35

Production and Testing of Antimicrobial Peptides and Their Mimics

Published on: April 10, 2026

Methods for assessing the structure and function of cationic antimicrobial peptides.

Michelle Pate1, Jack Blazyk

  • 1Department of Biomedical Sciences, Ohio University College of Osteopathic Medicine, Athens, OH, USA.

Methods in Molecular Medicine
|April 26, 2008
PubMed
Summary

Novel antimicrobial peptides that form beta-sheets, not alpha-helices, show improved selectivity for bacterial membranes. This offers a promising new strategy for combating antibiotic resistance and developing effective antimicrobial therapies.

More Related Videos

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
10:13

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization

Published on: August 11, 2018

Related Experiment Videos

Last Updated: Jul 5, 2026

Production and Testing of Antimicrobial Peptides and Their Mimics
10:35

Production and Testing of Antimicrobial Peptides and Their Mimics

Published on: April 10, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
10:13

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization

Published on: August 11, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Rising antibiotic resistance necessitates novel antimicrobial therapies.
  • Naturally occurring cationic peptides are part of innate immunity but often lack clinical efficacy due to poor selectivity.
  • Existing antimicrobial peptides commonly adopt an alpha-helical structure, which can lead to host cell damage.

Purpose of the Study:

  • To introduce a new strategy for designing antimicrobial peptides.
  • To investigate the structure and function of novel beta-sheet forming cationic antimicrobial peptides.
  • To evaluate the enhanced selectivity of these peptides for bacterial versus mammalian cell membranes.

Main Methods:

  • Design and synthesis of linear cationic peptides.
  • Structural analysis to confirm amphipathic beta-sheet formation.
  • Functional assays to assess membrane binding selectivity and lytic activity.

Main Results:

  • Developed novel cationic antimicrobial peptides that form amphipathic beta-sheets.
  • These beta-sheet peptides demonstrated superior selectivity for bacterial plasma membranes over mammalian membranes.
  • This improved selectivity addresses a key limitation of previous antimicrobial peptide designs.

Conclusions:

  • Antimicrobial peptides forming beta-sheets represent a promising alternative to alpha-helical designs.
  • The enhanced selectivity of beta-sheet peptides offers potential for safer and more effective antimicrobial therapies.
  • Further evaluation of these peptides is warranted for clinical applications against infectious diseases.