Investigating the Specificity of the Dehydration and Cyclization Reactions in Engineered Lanthipeptides by Synechococcal SyncM DOI Creative Commons
Patricia Arias-Orozco, Yunhai Yi, Fleur Ruijne

et al.

ACS Synthetic Biology, Journal Year: 2022, Volume and Issue: 12(1), P. 164 - 177

Published: Dec. 15, 2022

ProcM-like enzymes are class II promiscuous lanthipeptide synthetases that an attractive tool in synthetic biology for producing lanthipeptides with biotechnological or clinically desired properties. SyncM is a recently described modification enzyme from this family used to develop versatile expression platform engineering lanthipeptides. Most remarkably, can modify up 79 SyncA substrates single strain. Six SyncAs were previously characterized pool of substrates. They showed particular characteristics, such as the presence one two lanthionine rings, different flanking residues influencing ring formation, and directions, demonstrating relaxed specificity toward its precursor peptides. To gain deeper understanding potential biosynthetic tool, we further explored enzyme′s capabilities limits dehydration formation. We scaffolds peptide engineering, including changes ring′s directionality (relative position Ser/Thr Cys peptide) size. aimed rationally design mimetics cyclic antimicrobials introduce macrocycles prochlorosin-related nonrelated This study highlights largest 15 amino acids (ring-forming included) date. Taking advantage acid substrate tolerance SyncM, designed first single-SyncA-based antimicrobial. The insights gained work will aid future bioengineering studies. Additionally, it broadens SyncM′s application scope introducing other bioactive molecules.

Language: Английский

Harnessing the Power of Bacteriocins: A Comprehensive Review on Sources, Mechanisms, and Applications in Food Preservation and Safety DOI
Bhupendra Pratap Singh, Nishant Kumar, Ashok Yadav

et al.

Current Microbiology, Journal Year: 2025, Volume and Issue: 82(4)

Published: March 7, 2025

Language: Английский

Citations

0
Nano delivery platforms for nisin, a potent cyclic peptide: a comprehensive review of biological applications DOI

Alan Joy,

Nithesh Jerome,

Saraswathi Ramakrishnan

et al.

Polymer Bulletin, Journal Year: 2025, Volume and Issue: unknown

Published: March 17, 2025

Language: Английский

Citations

0
The untapped potential of actinobacterial lanthipeptides as therapeutic agents DOI Creative Commons

Dulce Ramírez-Rendón,

Fernando Guzmán‐Chávez, Carlos García-Ausencio

et al.

Molecular Biology Reports, Journal Year: 2023, Volume and Issue: 50(12), P. 10605 - 10616

Published: Nov. 7, 2023

Abstract The increase in bacterial resistance generated by the indiscriminate use of antibiotics medical practice set new challenges for discovering bioactive natural products as alternatives therapeutics. Lanthipeptides are an attractive product group that has been only partially explored and shows engaging biological activities. These molecules small peptides with potential application therapeutic agents. Some members show antibiotic activity against problematic drug-resistant pathogens a wide variety viruses. Nevertheless, their activities not restricted to antimicrobials, contribution treatment cystic fibrosis, cancer, pain symptoms, control inflammation, blood pressure demonstrated. study biosynthetic gene clusters through genome mining contributed accelerating discovery, enlargement, diversification this products. In review, we provide insight into recent advances development research actinobacterial lanthipeptides hold great

Language: Английский

Citations

8
Mining and Biosynthesis of Bioactive Lanthipeptides From Microorganisms DOI Creative Commons
Caiyun Li, Khorshed Alam, Yiming Zhao

et al.

Frontiers in Bioengineering and Biotechnology, Journal Year: 2021, Volume and Issue: 9

Published: July 29, 2021

Antimicrobial resistance is one of the most serious public health issues in worldwide and only a few new antimicrobial drugs have been discovered recent decades. To overcome ever-increasing emergence multidrug-resistant (MDR) pathogens, discovery natural products (NPs) against MDR pathogens with technologies great demands. Lanthipeptides which are ribosomally synthesized post-translationally modified peptides (RiPPs) display high diversity their chemical structures mechanisms action. Genome mining biosynthetic engineering also yielded lanthipeptides, valuable source drug candidates. In this review we cover advances field microbial derived lanthipeptide development.

Language: Английский

Citations

19
Investigating the Specificity of the Dehydration and Cyclization Reactions in Engineered Lanthipeptides by Synechococcal SyncM DOI Creative Commons
Patricia Arias-Orozco, Yunhai Yi, Fleur Ruijne

et al.

ACS Synthetic Biology, Journal Year: 2022, Volume and Issue: 12(1), P. 164 - 177

Published: Dec. 15, 2022

ProcM-like enzymes are class II promiscuous lanthipeptide synthetases that an attractive tool in synthetic biology for producing lanthipeptides with biotechnological or clinically desired properties. SyncM is a recently described modification enzyme from this family used to develop versatile expression platform engineering lanthipeptides. Most remarkably, can modify up 79 SyncA substrates single strain. Six SyncAs were previously characterized pool of substrates. They showed particular characteristics, such as the presence one two lanthionine rings, different flanking residues influencing ring formation, and directions, demonstrating relaxed specificity toward its precursor peptides. To gain deeper understanding potential biosynthetic tool, we further explored enzyme′s capabilities limits dehydration formation. We scaffolds peptide engineering, including changes ring′s directionality (relative position Ser/Thr Cys peptide) size. aimed rationally design mimetics cyclic antimicrobials introduce macrocycles prochlorosin-related nonrelated This study highlights largest 15 amino acids (ring-forming included) date. Taking advantage acid substrate tolerance SyncM, designed first single-SyncA-based antimicrobial. The insights gained work will aid future bioengineering studies. Additionally, it broadens SyncM′s application scope introducing other bioactive molecules.

Language: Английский

Citations

13