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

Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

2.5K
Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
2.5K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

4.3K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
4.3K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K

You might also read

Related Articles

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

Sort by
Same author

Accurate and task-agnostic modeling of enzymatic reactions through multimodal relational learning.

Acta pharmaceutica Sinica. B·2026
Same author

The "efficacy window" phenomenon of daridorexant in insomnia treatment: a dose-dependent time-course meta-analysis.

Frontiers in pharmacology·2026
Same author

Comparative transcriptomics identifies ribosome-associated signatures associated with restricted replication of wild-type infectious bronchitis virus in DF-1 cells.

Microbial pathogenesis·2026
Same author

Glucagon-like peptide-1 improves vascular endothelial dysfunction in hypertensive mice via CREB-driven transcriptional regulation of long non-coding RNA 155383.

British journal of pharmacology·2026
Same author

Physical and mental health impact of perimenopause, menopause and post menopause in a diverse global population (MARIE Project- Global Chapter WP 2a): cross-sectional quantitative data from a mixed-methods study.

EClinicalMedicine·2026
Same author

Corrigendum to "Evaluation methods of pressure injury stages: A systematic review and meta-analysis" [J Tissue Viability 34 3100894 (2025)].

Journal of tissue viability·2026

Related Experiment Video

Updated: Sep 18, 2025

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids
10:23

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

Published on: May 3, 2024

1.0K

Matrix metalloproteinase-triggered self-assembling peptides for biomedical applications.

Zhuyun Liu1, Chunlin Yu1,2, Zhenjia Li1

  • 1School of Life Science, Liaoning Normal University, Dalian 116081, China.

Journal of Materials Chemistry. B
|June 24, 2025
PubMed
Summary

Matrix metalloproteinases (MMPs) trigger peptide self-assembly into hydrogels and nanostructures. These advanced biomaterials show promise for targeted drug delivery and tissue regeneration, offering new therapeutic strategies.

More Related Videos

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K
Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
05:24

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

1.3K

Related Experiment Videos

Last Updated: Sep 18, 2025

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids
10:23

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

Published on: May 3, 2024

1.0K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K
Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
05:24

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

1.3K

Area of Science:

  • Biomaterials Science
  • Biomedical Engineering
  • Molecular Biology

Background:

  • Matrix metalloproteinases (MMPs) are crucial enzymes involved in physiological processes, with altered levels linked to various diseases.
  • Peptide self-assembly into hydrogels and nanomaterials is a key area in biomedical research.
  • MMPs can initiate specific peptide assemblies for diverse therapeutic applications.

Purpose of the Study:

  • To review the applications of MMP-triggered self-assembled peptide hydrogels and nanostructures.
  • To highlight their potential in controlled drug delivery, targeted therapy, and wound healing.
  • To discuss future opportunities and challenges in this field.

Main Methods:

  • Review of scientific literature on MMP-triggered peptide self-assembly over the past decade.
  • Analysis of applications in disease treatment and tissue engineering.
  • Evaluation of nanostructures for sensing and controlled substance release.

Main Results:

  • MMP-triggered peptide assemblies form hydrogels and nanostructures with significant biomedical potential.
  • These materials are effective in cancer therapy, inflammation management, wound healing, and tissue engineering.
  • Enzyme-cleavable sequences enable targeted drug release and enhanced functionality.

Conclusions:

  • MMP-triggered peptide self-assembly offers a versatile platform for advanced biomaterials.
  • These materials hold great promise for intelligent drug delivery and regenerative medicine.
  • Further research is needed to overcome challenges and fully realize their therapeutic potential.