Lasso Peptide

lasso peptide

Lasso peptides are a new class of natural products that have gained interest for their diverse biological activities. They are characterized by a macrocyclic ring that contains a C-terminal tail. These peptides contain a high degree of proteolytic stability and antimicrobial activity.

Lasso peptides belong to the natural product superfamily of RiPPs. The ring is a key feature to their highly compact structure and their intrinsic antibacterial properties. Despite their unique structural features, lasso peptides are posttranslationally modified. This process may be responsible for their broad range of biological activity.

Various research groups have investigated the biosynthesis and maturation of lasso peptides. One study focused on microcin J25, which was isolated from E. coli. Another group studied the production of lasso peptides in Streptomyces leeuwenhoekii C34T.

LASSO PEPTEX: LASSO peptides are a promising candidate for medical applications. Their thermal and antimicrobial stability make them ideal drug carriers and agonists of cell surface receptors. A variety of lasso peptides have been designed using recombinant genetics.

LASSO peptides are ribosomally synthesized, and the macrocyclic ring is formed from seven to nine N-terminal amino acid residues. However, a disulfide bond forms between the macrocyclic ring and the tail. The resulting peptide is classified into four classes based on the number of disulfide bonds. Class IV lasso peptides contain one disulfide bond. Classes III and II lasso peptides have no disulfide bonds.

Some researchers have suggested that GntR-family regulators play an important role in regulating the production of lasso peptides. However, the regulation of lasso peptides in native hosts is not fully understood.


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