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

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

You might also read

Related Articles

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

Sort by
Same author

ERK autoinhibition mechanism informs a drug combination strategy.

Protein science : a publication of the Protein Society·2026
Same author

Energy landscapes in molecular biology: History, principles, and perspectives.

Quarterly reviews of biophysics·2026
Same author

Introduction to "Endocytosis and cellular delivery".

RSC chemical biology·2026
Same author

Interactions of POPC Liposomes with Graphene Investigated by Quartz Crystal Microbalance and All-Atom Molecular Dynamics Simulations.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Leveraging conformational ensembles in allosteric drug discovery.

Trends in pharmacological sciences·2026
Same author

Allosteric drugs in biomolecular condensates: ways forward.

Drug discovery today·2026
Same journal

A Domino-Synthesized Dicoordinate Copper(I) Bis-imidazopyridine Complex Triggering Cuproptosis/Ferroptosis for Enhanced Cancer Immunotherapy.

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

Mirror-Symmetric Organic Two-Dimensional Crystals for Alternative Photon Transport Pathways.

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

Cobalt-Catalyzed Migratory E-Selective Asymmetric Aza-Nozaki-Hiyama-Kishi Coupling.

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

Facile Synthesis of α,ω-Dihydroxy Telechelic Macromonomers From Ethylene and α-Olefins for Recyclable Alternating Block Copolymers.

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

Multi-Atom Sub-Nanometer Assemblies on Interpenetrating Multi-Chambered N/C Nanospheres.

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

A Synergistic C<sub>2+</sub> Alcohols/Olefins-Intermediated Pathway Boosts CO<sub>2</sub> Hydrogenation to Aromatics.

Angewandte Chemie (International ed. in English)·2026
See all related articles

Related Experiment Video

Updated: Jun 16, 2026

Author Spotlight: Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
06:45

Author Spotlight: Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

2.1K

A Photo-Switchable Peptide Fibril Esterase.

Mousumi Samanta1,2, Noy Saad1, Dinghao Wu3

  • 1Chemistry Department, Ben-Gurion University of the Negev, Campus st. 1, Beer Sheva, 8410501, Israel.

Angewandte Chemie (International Ed. in English)
|September 27, 2024
PubMed
Summary
This summary is machine-generated.

Researchers developed a light-responsive peptide catalyst that can be switched on and off using UV and visible light. This photo-switchable catalyst mimics enzyme activity and offers precise control for nanotechnology applications.

Keywords:
Dynamic self-assemblyLight triggeringPeptide catalysisStereoselective catalysisSystems Chemistry

More Related Videos

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
19:23

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation

Published on: January 16, 2019

9.2K
A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
07:53

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

33.1K

Related Experiment Videos

Last Updated: Jun 16, 2026

Author Spotlight: Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
06:45

Author Spotlight: Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

2.1K
Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
19:23

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation

Published on: January 16, 2019

9.2K
A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
07:53

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

33.1K

Area of Science:

  • Supramolecular Chemistry
  • Catalysis
  • Peptide Nanotechnology

Background:

  • Mimicking enzyme catalysis with peptide catalysts enhances reactions but lacks external regulation.
  • Light irradiation offers precise temporal and spatial control for molecular functionality.
  • Photo-switchable molecules are ideal for on-demand regulation in various reaction media.

Purpose of the Study:

  • To select and characterize a photo-switchable amphiphilic peptide catalyst.
  • To investigate the light-induced regulation of catalytic activity in peptide assemblies.
  • To explore the potential of reversible peptide self-assembly for nanotechnology.

Main Methods:

  • Selection of isomeric peptides containing azobenzene and histidine residues.
  • Investigation of UV and visible light effects on peptide fibril disassembly and reassembly.
  • Enantioselective ester hydrolysis assays to quantify catalytic activity.

Main Results:

  • A photo-switchable peptide catalyst was selected, exhibiting efficient enantioselective ester hydrolysis in fibrillar form.
  • UV light-induced trans-to-cis azobenzene isomerization disassembled fibrils, significantly reducing catalytic activity.
  • Catalytic activity was reversibly restored upon visible light irradiation, enabling multiple on/off cycles.

Conclusions:

  • Photo-switchable peptide catalysts offer precise, light-mediated control over catalytic function.
  • Reversible self-assembly and disassembly of peptide fibrils can be triggered by light.
  • This research provides insights into early chemical evolution and advances peptide nanotechnology.