Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins
Delphine Nørgaard Møller1, Christian Kofoed1, Mikkel Boas Thygesen1
1Department of Chemistry, University of Copenhagen, Frederiksberg C, Denmark.
Summary
Peptide tags enable site-selective protein modification, overcoming limitations of conventional methods for creating protein conjugates. These tags facilitate covalent modifications without enzymes, advancing bioconjugation chemistry applications.
Area of Science:
- Bioconjugation Chemistry
- Chemical Biology
- Protein Engineering
Background:
- Bioconjugation chemistry is crucial for protein studies and pharmaceutical development.
- Traditional protein functionalization methods often lack regioselectivity.
- Site-selective modification is key for synthesizing precise protein conjugates.
Purpose of the Study:
- To review advances in peptide tags for site-selective protein modification.
- To highlight applications of peptide tags in bioconjugation.
- To discuss modifications proceeding without enzymatic assistance.
Main Methods:
- Review of literature on peptide tag development.
- Analysis of applications in protein conjugation.
- Focus on non-enzymatic covalent modification strategies.
Main Results:
- Peptide tags offer improved regioselectivity in protein functionalization.
- Minimal protein mutation is achievable with these tags.
- Successful applications in synthesizing complex protein conjugates.
Conclusions:
- Peptide tags are valuable tools for site-selective protein modification.
- These tags minimize interference with native protein properties.
- Advances in peptide tags expand bioconjugation possibilities.
Related Concept Videos
01:24Tagging and Fusion Proteins
8.3K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
8.3K
02:04Covalently Linked Protein Regulators
8.7K
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....
8.7K
02:04Covalently Linked Protein Regulators
2.0K
2.0K
02:43Peptide Bonds
82.1K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
82.1K
01:32Lipids as Anchors
7.2K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
7.2K
00:49Ligand Binding and Linkage
5.5K
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...
5.5K