LASSO Peptide is a group of post-translational peptides with remarkable thermal and protease stability. These peptides possess diverse biological activities and are suitable for functional engineering. They are also highly promising candidates for medical applications.
The lasso peptide has a unique 3D-interlocked structure. It is composed of an N-terminal macrolactam ring threaded by a linear C-terminal part. The lasso peptides are ribosomally biosynthesized using naturally occurring L-amino acids.
LASSO Peptides have emerged as a new class of natural peptides. They are characterized by their post-translational modifications, which are achieved through dedicated enzymatic machinery. They have unique biological activities such as antimicrobial, anticancer, and receptor antagonistic properties. These peptides have been used as molecular probes in medical applications.
Lasso peptides are classified into four classes. The lasso peptides with one disulfide bond are class I, while those with two are class II. Those with a single disulfide bond are class III. They have a tertiary tail.
The lasso peptides are produced from a linear precursor called LasA. It is synthesized by the LasA synthetase which is made up of proteins B and C. The LasA peptides are cyclized into a macrolactam ring by the lasso cyclase (C). The cyclase catalyzes the formation of the macrolactam, which is then released as the core peptide. The N-terminal lasso peptide is released through a mechanism that involves the cleavage of the leader peptide. During maturation, the lasso peptide undergoes a cyclization, in which the macrolactam ring and the tail are joined by a disulfide bond.