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Lasso Peptides: Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds (SpringerBriefs in Microbiology) by Yanyan Li; Séverine Zirah; Sylvie Rebuffat is a scholarly article available to read on EtoBox.

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Lasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on d

Author

Yanyan Li; Séverine Zirah; Sylvie Rebuffat

Publisher

Springer New York : Imprint Springer, Springer New York, Imprint Springer

Published

2015

Language

EN

ISBN

9781493910106