Related Experiment Video
Updated: May 10, 2026
09:45
Modification and Functionalization of the Guanidine Group by Tailor-made Precursors
Published on: April 27, 2017
A molecular toolkit for the functionalization of titanium-based biomaterials that selectively control
Florian Rechenmacher1, Stefanie Neubauer, Carlos Mas-Moruno
1Institute for Advanced Study and Center for Integrated Protein Science, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.
Chemistry (Weinheim an Der Bergstrasse, Germany)
|June 8, 2013
Summary
We developed a click chemistry toolkit to precisely control cell adhesion on titanium materials by targeting specific integrins (α5β1 or αvβ3). This innovation enables selective cell binding, advancing biomaterial development and cell adhesion studies.
Area of Science:
- Biomaterials Science
- Cell Biology
- Surface Chemistry
Background:
- Integrin-mediated cell adhesion is crucial for biological processes.
- Controlling specific integrin subtypes (e.g., α5β1, αvβ3) on biomaterials remains a challenge.
- Titanium-based materials are widely used in biomedical applications.
Purpose of the Study:
- To create a molecular toolkit for biofunctionalizing titanium materials.
- To achieve selective control over integrin-mediated cell adhesion.
- To develop surfaces that can discriminate between α5β1 and αvβ3 integrin binding.
Main Methods:
- Utilized click chemistry for covalent immobilization of RGD peptidomimetics on titanium surfaces.
- Employed solid-phase integrin binding assays to evaluate α5β1 binding affinity and selectivity.
- Screened phosphonic acid-containing anchoring units for optimal titanium surface binding and integrin interaction.
- Validated surface specificity using genetically modified fibroblasts expressing specific integrins.
Main Results:
- Achieved a nine-fold increase in α5β1 integrin affinity compared to controls.
- Demonstrated complete selectivity against αvβ3 integrin binding on functionalized surfaces.
- Successfully shifted cellular specificity by switching between α5β1- and αvβ3-selective peptidomimetics.
- Established the first Ti-based materials with controlled discrimination between α5β1 and αvβ3 integrin adhesion.
Conclusions:
- The click chemistry toolkit provides unprecedented control over integrin-mediated cell adhesion on titanium.
- These bioactive surfaces are valuable tools for studying integrin roles in biological events.
- The developed methodology facilitates the creation of novel biomaterials for targeting specific cell types.
Related Concept Videos
01:10Integrins
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
01:17Intracellular Signaling Affects Focal Adhesions
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
01:15Activation of Integrins
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
01:24Overview of Cell-Matrix Interactions
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
01:20Cell Adhesion Molecules - Types and Functions
Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily involved in a...
CAM Families
The Integrin family of proteins is primarily involved in a...