Related Experiment Video
Updated: Mar 29, 2026

07:11
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
3.2K
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization
Giang K T Nguyen1, Antony Kam1, Shining Loo1
1School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore.
Journal of the American Chemical Society
|December 4, 2015
Summary
A new method using butelase 1 rapidly macrocyclizes peptides and proteins. This efficient protein cyclization technique is 20,000 times faster than current methods, achieving high yields in minutes.
Area of Science:
- Biochemistry
- Molecular Biology
- Drug Discovery
Background:
- Macrocyclization is crucial for developing new drugs and engineering proteins.
- Existing methods for macrocycle synthesis often lack general applicability and efficiency.
Purpose of the Study:
- To develop a highly efficient and general method for peptide and protein macrocyclization.
- To compare the efficiency of the new method with existing protein cyclization techniques.
Main Methods:
- Utilized butelase 1 for the macrocyclization of peptides and proteins.
- Tested the method across a range of protein sizes (26 to >200 residues).
Main Results:
- Achieved highly efficient macrocyclization of peptides and proteins.
- Demonstrated reaction rates 20,000 times faster than sortase A-mediated cyclization.
- Obtained yields up to 95% with reactions completing within minutes.
Conclusions:
- Butelase 1 offers a significantly faster and more efficient approach to protein and peptide macrocyclization.
- This method provides a valuable new tool for drug design and protein engineering applications.
- The speed and efficiency of butelase 1 overcome limitations of current protein cyclization strategies.
Related Concept Videos
Peptide Bonds
86.5K
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...
86.5K
Ligand Binding and Linkage
6.0K
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...
6.0K
Bacterial Protein Maturation
701
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
701
The Proteasome
2.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among 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. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
2.0K
Protein Folding
12.5K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.5K

