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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.6K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.6K
Ligand Binding Sites02:40

Ligand Binding Sites

14.9K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
14.9K
Antimicrobial Proteins01:23

Antimicrobial Proteins

13.0K
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...
13.0K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.7K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.5K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.5K

You might also read

Related Articles

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

Sort by
Same author

Deep Learning Enables Identification of Antimicrobial Peptides Through Mechanochromic Fingerprints.

Angewandte Chemie (International ed. in English)·2026
Same author

Novel Biomaterial-Based Synovial Fluid Analysis Reveals Protective microRNA Signatures in a Mouse Model of Acute Synovitis-Driven Osteoarthritis.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2026
Same author

Aggregation-State Dynamics Drive Double Cooperativity Between Antimicrobial Peptides LL-37 and HNP1.

Angewandte Chemie (International ed. in English)·2026
Same author

Heteroaggregation of Antimicrobial Peptides LL-37 and HNP‑1 Drives Cooperative Neutralization of Cytotoxicity.

JACS Au·2026
Same author

Rheological and thermal behaviour of microtubule networks mediated by microtubule associated proteins.

Soft matter·2025
Same author

A QCM-Based Biosensor to Detect HIT-like Antibodies: Differentiating KKO from RTO via FcγRIIA Interactions.

Analytical chemistry·2025

Related Experiment Video

Updated: Jan 16, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

13.0K

Single Amino Acid Modulates Antimicrobial Peptide Cooperativity between LL-37 and HNP1.

Ariane M Schwitter1, Takashi Yasuda2, Xiang Li2

  • 1Institute of Industrial Science, The University of Tokyo, 4-6-1 Komaba Meguro-Ku, Tokyo 153-8505, Japan.

Langmuir : the ACS Journal of Surfaces and Colloids
|January 15, 2026
PubMed
Summary

Human antimicrobial peptides (AMPs) like LL-37 and defensins show synergistic effects against resistant bacteria. Defensin N-termini are key to this cooperative interaction, enhancing bacterial killing and reducing host toxicity.

More Related Videos

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

10.0K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.5K

Related Experiment Videos

Last Updated: Jan 16, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

13.0K
Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
08:09

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

10.0K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.5K

Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Antimicrobial peptides (AMPs) are crucial in combating multidrug-resistant bacterial infections.
  • Human AMPs LL-37 and α-defensin (HNP1) demonstrate synergistic activity, enhancing bacterial killing and reducing host cell toxicity.
  • The structural basis for this cooperative phenomenon between LL-37 and defensins is not well understood.

Purpose of the Study:

  • To investigate the structural-function relationship underlying the cooperative effect between LL-37 and various defensins.
  • To determine if the observed cooperative effect between LL-37 and HNP1 is specific or extends to other defensin family members.
  • To identify specific regions within defensins responsible for modulating the synergistic interaction with LL-37.

Main Methods:

  • Membrane toxicity assays were performed to assess the interaction between LL-37 and different defensins (HNP1, HNP3, HNP4, hBD1, HNP2).
  • Comparative analysis of amino acid sequences of various defensins was conducted.
  • Structure-activity relationship studies focused on the N-terminal regions of defensins.

Main Results:

  • The cooperative effect of LL-37 neutralization against POPC membranes by HNP1 was observed with HNP3, HNP4, and hBD1, but not HNP2.
  • The N-terminal region of defensins was identified as a critical modulator of the cooperative effect with LL-37.
  • Specific amino acid variations in the N-terminus correlated with the presence or absence of the synergistic interaction.

Conclusions:

  • The cooperative interaction between LL-37 and defensins is not limited to HNP1 but is a broader property of certain defensin family members.
  • The N-terminus of defensins plays a pivotal role in mediating the synergistic antimicrobial activity and reduced cytotoxicity when combined with LL-37.
  • Understanding this structural-function relationship can guide the development of novel AMP-based therapeutics.