Related Experiment Video
Updated: Jan 7, 2026
07:11
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
3.1K
Site-Selective Protein Modification via Peptide-Directed Proximity Catalysis.
Laetitia Raynal1,2, Joe Nabarro1,2, Lisa M Miller2,3
1Department of Chemistry, University of York, Heslington YO10 5DD, U.K.
ACS Omega
|January 5, 2026
Summary
Catalyst-functionalized peptides enable precise protein modification through proximity catalysis. Researchers can tune modification sites by altering peptide-catalyst structure for diverse applications.
Area of Science:
- Biochemistry
- Chemical Biology
- Protein Engineering
Background:
- Proximity catalysis enables localized protein modification via ligand binding.
- Developing versatile ligands is key for advancing this technique.
Purpose of the Study:
- Introduce catalyst-functionalized peptides as adaptable ligands for proximity catalysis.
- Demonstrate site-selective protein modification using these novel peptide ligands.
Main Methods:
- Functionalized target-binding peptides with pyridinium oxime catalysts.
- Utilized N-acyl-N-alkylsulfonamide reagents for protein modification.
- Investigated the impact of catalyst position on modification site.
Main Results:
- Achieved site-selective modification of model proteins.
- Successfully introduced functionalities like fluorophores and affinity handles.
- Demonstrated that altering catalyst position on the peptide tunes the modification site.
Conclusions:
- Catalyst-functionalized peptides are effective ligands for proximity catalysis.
- Peptide-catalyst design offers control over protein modification sites.
- This approach facilitates the development of tailored protein modification strategies.
More Related Videos
Related Concept Videos
00:49Ligand Binding and Linkage
5.4K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.4K
02:04Covalently Linked Protein Regulators
8.6K
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....
8.6K
01:19Allosteric Proteins-ATCase
6.4K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.4K
02:40Ligand Binding Sites
14.8K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
14.8K
01:26Protein Modifications in the RER
6.8K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.8K
02:18The Proteasome
10.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.0K