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Lasso peptide, a highly stable structure and designable multifunctional backbone

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Abstract

Lasso peptide belongs to a new class of natural product with highly compact and stable structure. It has varieties of biological activities, among which the most important one is its antibacterial efficacy. Novel lasso peptides have been constantly discovered and analyzed by advanced techniques, and the biosynthesis or even chemical synthesis of lasso peptide has been studied after learning its constituent amino acids and maturation process. Structural identification of lasso peptide provides information for elucidating the mechanisms of its antibacterial activity and basis for further modifications. Ring of lasso peptide is the key to both its highly compact and stable structure and its intrinsic antibacterial property. The loop has been considered as suitable modification region of lasso peptide, such as V11–S18 of MccJ25 being modifiable without disrupting the lasso structure in biosynthesis. The tail is the immunity protein that can export lasso peptide out of its produced strain and serve as a self-protection mechanism at the same time. Most of currently known lasso peptides are non-pathogenic, which implies that the modified lasso peptides are promising candidates for medical applications. Arginine, glycine, and aspartic acid as a ligands of cancer-specific receptor have been grafted to the loop of lasso peptide without losing its bioactivity, and many other targets are expected to be used for lasso peptide modification. Multi-molecular modification and large-scale production need to be studied and solved in future for designing and using multifunctional lasso peptide based on its extraordinary stable structure.

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Acknowledgments

This work was supported in part by the Fundamental Research Funds for Central Universities of China (N142003001, N130520001), the Natural Science Foundation of China (81201141), and the Office of Science (BER), US Department of Energy (DE-SC0008397).

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    1. Institute of Molecular Medicine, College of Life and Health Sciences, Northeastern University, Shenyang, 110000, China

      Ning Zhao, Yongxu Pan & Hongguang Liu

    2. Department of Radiology, Molecular Imaging Program at Stanford (MIPS), Bio-X Program and Stanford Cancer Center, Stanford University School of Medicine, Stanford, CA, 94305, USA

      Zhen Cheng

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    N. Zhao and Y. Pan contributed equally to the work.

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    Zhao, N., Pan, Y., Cheng, Z. et al. Lasso peptide, a highly stable structure and designable multifunctional backbone. Amino Acids 48, 1347–1356 (2016). https://doi.org/10.1007/s00726-016-2228-x

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