SpringerBriefs in Microbiology

Lasso Peptides

Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds

Authors: Li, Yanyan, Zirah, Séverine, Rebuffat, Sylvie

  • Expanding field of research
  • Focus on lasso peptides
  • Explores the therapeutic uses of lasso peptides
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Softcover $54.99
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About this book

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 different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies.

Table of contents (5 chapters)

  • Introduction: A Review of Lasso Peptide Research

    Li, Yanyan (et al.)

    Pages 1-6

  • From the Producer Microorganisms to the Lasso Scaffold

    Li, Yanyan (et al.)

    Pages 7-35

  • Biological Activities of Lasso Peptides and Structure–Activity Relationships

    Li, Yanyan (et al.)

    Pages 37-79

  • Biosynthesis, Regulation and Export of Lasso Peptides

    Li, Yanyan (et al.)

    Pages 81-95

  • Lasso Peptide Bioengineering and Bioprospecting

    Li, Yanyan (et al.)

    Pages 97-103

Buy this book

eBook $39.99
price for USA (gross)
  • ISBN 978-1-4939-1010-6
  • Digitally watermarked, DRM-free
  • Included format: EPUB, PDF
  • ebooks can be used on all reading devices
  • Immediate eBook download after purchase
Softcover $54.99
price for USA
  • ISBN 978-1-4939-1009-0
  • Free shipping for individuals worldwide
  • Usually dispatched within 3 to 5 business days.
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Bibliographic Information

Bibliographic Information
Book Title
Lasso Peptides
Book Subtitle
Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds
Authors
Series Title
SpringerBriefs in Microbiology
Copyright
2015
Publisher
Springer-Verlag New York
Copyright Holder
Yanyan Li, Séverine Zirah and Sylvie Rebuffat
eBook ISBN
978-1-4939-1010-6
DOI
10.1007/978-1-4939-1010-6
Softcover ISBN
978-1-4939-1009-0
Series ISSN
2191-5385
Edition Number
1
Number of Pages
XIII, 103
Number of Illustrations and Tables
13 b/w illustrations, 9 illustrations in colour
Topics