Related Experiment Video
Updated: May 30, 2026
08:01
Synthesis of Monocyte-targeting Peptide Amphiphile Micelles for Imaging of Atherosclerosis
Published on: November 17, 2017
pH influenced molecular switching with micelle bound cavitands
Yeon Joo Kim1, Mark T Lek, Michael P Schramm
1California State University Long Beach, Department of Chemistry and Biochemistry, 1250 Bellflower Blvd., Long Beach, CA 90840, USA.
Chemical Communications (Cambridge, England)
|August 3, 2011
Summary
pH-responsive resorcinarene host-guest complexes were created. Amphiphilic guests flip 180° within the host due to charge changes, demonstrating tunable molecular recognition.
Area of Science:
- Supramolecular Chemistry
- Host-Guest Chemistry
- Molecular Recognition
Background:
- Resorcinarene hosts are known for their ability to encapsulate guest molecules.
- Amphiphilic molecules possess both hydrophilic and hydrophobic properties.
- pH is a critical factor influencing molecular interactions and conformations.
Purpose of the Study:
- To develop novel resorcinarene host-amphiphilic guest complexes.
- To investigate the influence of pH on guest orientation within the host.
- To demonstrate switchable molecular recognition based on pH stimuli.
Main Methods:
- Synthesis of resorcinarene derivatives and functionalized amphiphilic guests.
- Formation of host-guest complexes.
- pH titration and spectroscopic analysis (e.g., NMR) to determine guest orientation.
- Computational modeling to understand interaction mechanisms.
Main Results:
- Successfully formed resorcinarene-amphiphilic guest complexes.
- Demonstrated a significant pH-dependent change in guest orientation within the host cavity.
- Observed a 180° orientation switch for guests with trimethylammonium and tert-butyl groups.
- Correlated guest orientation changes with the buildup of negative charge on the cavitand host.
Conclusions:
- pH is a powerful tool for controlling guest orientation in resorcinarene hosts.
- The developed complexes exhibit switchable recognition properties.
- This work provides a foundation for designing smart materials and sensors responsive to pH changes.
More Related Videos
Related Concept Videos
01:30Micelles
Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...
01:32Pinching-off of Coated Vesicles
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
01:42Phosphoinositides and PIPs
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
01:05Mechanism of Ciliary Motion
The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
01:39Mechanism of Filopodia Formation
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...