Related Experiment Video
Updated: May 10, 2026

Molecular Spring Constant Analysis by Biomembrane Force Probe Spectroscopy
Published on: November 20, 2021
Sequential binding of large molecules to hairy MOFs
Gonghua Wang1, Zhanping Xu, Ziguang Chen
1Department of Mechanical and Materials Engineering, University of Nebraska, Lincoln, Nebraska 68588, USA.
Researchers transformed smooth metal-organic frameworks (MOFs) into "hairy" structures using salts, boosting large molecule chemisorption 120-fold. Further etching enabled sequential protein binding, showcasing MOFs dynamic functional capabilities.
Area of Science:
- Materials Science
- Chemistry
- Nanotechnology
Background:
- Metal-organic frameworks (MOFs) exhibit dynamic properties.
- Controlling MOF surface morphology is crucial for advanced applications.
Purpose of the Study:
- To develop a simple method for transforming smooth MOF crystals into "hairy" structures.
- To enhance the chemisorption capacity of MOFs for large molecules.
- To enable sequential binding of different proteins onto MOF surfaces.
Main Methods:
- Treatment of MOF crystals with salts to induce morphological changes.
- Etching processes to further modify MOF structures.
- Chemisorption experiments to quantify molecular uptake.
- Protein binding assays to demonstrate sequential adsorption.
Main Results:
- Transformation of smooth MOFs into "hairy" MOFs via salt treatment.
- A 120-fold enhancement in chemisorption capacity for large molecules.
- Successful sequential adsorption of different proteins onto the modified MOFs.
Conclusions:
- Salt-induced morphological transformation is an effective strategy to enhance MOF functionality.
- Modified MOFs show significant potential for applications requiring high-capacity adsorption and selective binding, such as in separation and sensing.
- The developed method offers a facile route to engineer MOF surfaces for complex molecular interactions.
Related Concept Videos
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Ligand Binding and Linkage
Ligand Binding and Linkage
Cooperative Allosteric Transitions
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

