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

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

8.7K
Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
8.7K
Peptide Bonds02:43

Peptide Bonds

85.3K
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...
85.3K

You might also read

Related Articles

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

Sort by
Same author

Bioactive cationic lipidated oligomers (CLOs) as antimicrobial materials: metabolomic insights into MRSA membrane disruption.

Biomaterials science·2026
Same author

Hyperforin potentiates polymyxin B against multidrug-resistant Gram-negative pathogens via membrane disruption, biofilm eradication, and oxidative stress.

Antimicrobial agents and chemotherapy·2025
Same author

Structure-Activity Relationship of the Diaminobutyric Acid Residues in Polymyxins.

JACS Au·2025
Same author

Progress of AI-Driven Drug-Target Interaction Prediction and Lead Optimization.

International journal of molecular sciences·2025
Same author

Mycotoxin-Caused Intestinal Toxicity: Underlying Molecular Mechanisms and Further Directions.

Toxics·2025
Same author

The Detoxification Effects of Melatonin on Aflatoxin-Caused Toxic Effects and Underlying Molecular Mechanisms.

Antioxidants (Basel, Switzerland)·2025

Related Experiment Video

Updated: Mar 7, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

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

Published on: January 26, 2016

12.5K

Rediscovering the octapeptins.

Tony Velkov1, Kade D Roberts2, Jian Li3

  • 1Drug Development and Innovation, Drug Delivery, Disposition and Dynamics, Australia. Tony.Velkov@monash.edu.

Natural Product Reports
|February 10, 2017
PubMed
Summary
This summary is machine-generated.

Octapeptins are promising lipopeptide antibiotics effective against polymyxin-resistant superbugs. They offer a potential new class of drugs to combat difficult-to-treat Gram-negative infections.

More Related Videos

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
13:37

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

18.9K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.9K

Related Experiment Videos

Last Updated: Mar 7, 2026

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

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

Published on: January 26, 2016

12.5K
Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
13:37

Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

Published on: June 20, 2014

18.9K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.9K

Area of Science:

  • Microbiology
  • Medicinal Chemistry
  • Drug Discovery

Background:

  • Declining antibiotic discovery leads to widespread resistance.
  • Polymyxins (B and E/colistin) are last-resort treatments but face rising resistance.
  • Gram-negative pathogens like Pseudomonas aeruginosa, Acinetobacter baumannii, and Klebsiella pneumoniae are major threats.

Purpose of the Study:

  • To review the chemistry, antibacterial mechanisms, and biosynthesis of octapeptins.
  • To highlight octapeptins as potential alternatives to polymyxins.
  • To explore octapeptins for developing new antibiotics against resistant bacteria.

Main Methods:

  • Literature review of studies from 1975 to 2016.
  • Analysis of octapeptin structure-activity relationships.
  • Examination of biosynthesis pathways and resistance mechanisms.

Main Results:

  • Octapeptins are non-ribosomal lipopeptides with a distinct mechanism of action.
  • They exhibit no cross-resistance with polymyxins.
  • Octapeptins possess broad-spectrum activity, including against Gram-positive bacteria.

Conclusions:

  • Octapeptins represent a valuable resource for combating polymyxin-resistant Gram-negative infections.
  • Their unique properties make them ideal candidates for a new generation of lipopeptide antibiotics.
  • Further development of octapeptins could address the critical need for novel antibacterial agents.