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

Metal-Ligand Bonds02:51

Metal-Ligand Bonds

23.9K
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
23.9K
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

1.2K
In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
1.2K
Fibril-associated Collagen01:11

Fibril-associated Collagen

3.2K
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...
3.2K
Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

2.2K
Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...
2.2K
EDTA: Chemistry and Properties01:22

EDTA: Chemistry and Properties

3.2K
Polydentate ligands are most widely used in complexometric titrations because they form more stable complexes with the metal ions than mono- or bidentate ligands due to the chelate effect. Examples of polydentate ligands are ethylenediaminetetraacetic acid (EDTA), crown ethers, and cryptands. The most important feature of optimal polydentate ligands is the ability to form 1:1 complexes in a single-step process. Amino carboxylic acid derivatives are frequently used as complexing agents. EDTA is...
3.2K
Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

774
In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
774

You might also read

Related Articles

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

Sort by
Same author

A Macrocycle-Assisted Platform Approach to Protein Cross-Linking Via Chemically Inactive Residues.

Nano letters·2025
Same author

2D Materials Kill Bacteria from Within.

Nano letters·2024
Same author

Intracellularly Self-Assembled 2D Materials Induce Apoptotic Cell Death by Impeding Cytosolic Transport.

ACS nano·2023
Same author

Spiropyran-Appended Cucurbit[6]uril Enabling Direct Generation of 2D Materials inside Living Cells.

Small (Weinheim an der Bergstrasse, Germany)·2021
Same author

Evaluation of Mycoflora and Citrinin Occurrence in Chinese Liupao Tea.

Journal of agricultural and food chemistry·2020
Same author

Amount of Eurotium sp. in Chinese Liupao tea and its relationship with tea quality.

Journal of applied microbiology·2020

Related Experiment Video

Updated: Jan 11, 2026

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
07:12

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment

Published on: September 7, 2022

2.7K

Cross-linking Collagen Using Divalent Metal Ions.

Zhongyu Li1, Liping Pu1, Delong Hou1,2

  • 1Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, P. R. China.

Biomacromolecules
|November 19, 2025
PubMed
Summary
This summary is machine-generated.

Nontoxic divalent metal ions (M(II)) can now cross-link collagen, rivaling high-valent ions. This breakthrough uses engineered cucurbit[7]uril to enable biocompatible collagen materials with enhanced properties.

More Related Videos

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

17.7K
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

12.3K

Related Experiment Videos

Last Updated: Jan 11, 2026

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
07:12

Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment

Published on: September 7, 2022

2.7K
Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

17.7K
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

12.3K

Area of Science:

  • Biomaterials Science
  • Materials Chemistry
  • Biochemistry

Background:

  • Collagen cross-linking with high-valent metal ions enhances material properties but raises toxicity and stability concerns.
  • Divalent metal ions (M(II)) were previously ineffective for collagen cross-linking.

Purpose of the Study:

  • To demonstrate the efficacy of nontoxic divalent metal ions (M(II)) for collagen cross-linking.
  • To overcome limitations associated with high-valent metal ions in collagen-based materials.

Main Methods:

  • Engineered cucurbit[7]uril selectively binds to aromatic residues (Phe/Tyr) in collagen.
  • This binding creates specific coordination sites for divalent metal ions (M(II)).
  • Cross-linking efficiency and biocompatibility were assessed via in vitro experiments.

Main Results:

  • Divalent metal ions (M(II)), like Mg(II) and Ca(II), successfully cross-linked collagen.
  • Cross-linking efficiency matched or surpassed that of high-valent metal ions.
  • In vitro studies confirmed the nontoxic nature of M(II)-cross-linked collagen.

Conclusions:

  • Nontoxic divalent metal ions can effectively cross-link collagen using engineered cucurbit[7]uril.
  • This approach offers a safer alternative to high-valent metal ions for collagen modification.
  • Enables development of advanced, high-performance, biocompatible collagen materials.