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

5.0K
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...
5.0K

You might also read

Related Articles

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

Sort by
Same author

Synergistic Potential of Plant Alkaloids and Intragenic Antimicrobial Peptides in Treating Multidrug-Resistant Infectious Diseases.

Antibiotics (Basel, Switzerland)·2026
Same author

Cyclotides from Plants Driving the Next Generation of Antibacterial Agents.

Antibiotics (Basel, Switzerland)·2026
Same author

Green Synthesis of Magnesium Nanoparticles From Native Neotropical Savannah Plants For Scalable Nanophytocosmetic Formulations.

Journal of visualized experiments : JoVE·2026
Same author

Unraveling the mechanism of action of the PepGAT peptide against Candida albicans through proteomics approaches.

Scientific reports·2026
Same author

A computationally optimized peptide (KI17) derived from Talisia esculenta with potent action against multidrug-resistant pathogens.

Biochimica et biophysica acta. General subjects·2026
Same author

Cellular senescence in the dental pulp and its implications for endodontics: a scoping review.

Clinical oral investigations·2026
Same journal

Intrinsically disordered regions in eukaryotic mRNA decay pathways.

Trends in biochemical sciences·2026
Same journal

A unified mechanism of phosphate export across eukaryotes through EXS domain-containing proteins.

Trends in biochemical sciences·2026
Same journal

Drugging the proteome via large-scale chemoproteomics.

Trends in biochemical sciences·2026
Same journal

Peptideins: Navigating the gray zone of the proteome.

Trends in biochemical sciences·2026
Same journal

A metabolon channels nicotine biosynthesis.

Trends in biochemical sciences·2026
Same journal

Better call chaperone.

Trends in biochemical sciences·2026
See all related articles

Related Experiment Video

Updated: Sep 9, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K

Molecular design drives nanoarchitecture in self-assembling antimicrobial peptides.

Thuanny Borba Rios1, Mariana Rocha Maximiano1, Nelson Gomes de Oliveira Junior1

  • 1Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, Brasília, Distrito Federal, Brazil; S-Inova Biotech, Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, Mato Grosso do Sul, Brazil.

Trends in Biochemical Sciences
|August 31, 2025
PubMed
Summary
This summary is machine-generated.

Antimicrobial peptides (AMPs) show promise as alternatives to antibiotics. Their self-assembly into nanostructures enhances stability and efficacy, offering new strategies to combat infections.

Keywords:
antimicrobial peptides (AMPs)nanostructurespeptide-based therapeuticsphysicochemical interactionsself-assembly

More Related Videos

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.0K
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

7.4K

Related Experiment Videos

Last Updated: Sep 9, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.0K
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

7.4K

Area of Science:

  • Biochemistry
  • Materials Science
  • Microbiology

Background:

  • Antimicrobial peptides (AMPs) are a promising class of therapeutics due to their broad-spectrum activity and low resistance potential.
  • Peptide self-assembly is increasingly recognized for its role in improving AMP stability, bioavailability, and effectiveness.

Purpose of the Study:

  • To review the molecular mechanisms of antimicrobial peptide self-assembly.
  • To highlight how self-assembly influences AMP functionality and antimicrobial performance.
  • To discuss potential applications of self-assembled AMPs in combating infections.

Main Methods:

  • Review of current literature on antimicrobial peptide self-assembly.
  • Analysis of physicochemical factors influencing nanostructure formation (hydrophobicity, charge, aromatic interactions).
  • Examination of self-assembly's impact on AMP stability, membrane interaction, and bacterial disruption mechanisms.

Main Results:

  • Self-assembly via non-covalent interactions forms nanostructures (nanofibers, nanotubes, micelles).
  • Self-assembled AMPs exhibit enhanced stability, improved membrane interactions, and modulated bacterial disruption.
  • Tailoring physicochemical features allows for enhanced antimicrobial performance and controlled drug delivery.

Conclusions:

  • Peptide self-assembly is a key strategy for enhancing AMP efficacy and overcoming resistance.
  • Self-assembled AMPs offer potential for controlled release, targeted delivery, and synergistic antimicrobial approaches.
  • Further research into self-assembled AMPs could lead to novel treatments for infectious diseases.