Lugdunin features a cyclic peptide scaffold containing noncanonical residues that confer unique conformational and physicochemical properties. The structure displays notable rigidity, enabling detailed analysis of membrane-interactive behavior. Researchers utilize it to investigate peptide-derived antimicrobial mechanisms and structural mimicry. Broad utility spans peptide natural-product research and biosynthetic pathway studies.
CAT No: R2623
CAS No:1989698-37-4
Synonyms/Alias:lugdunin;1989698-37-4;CHEBI:133127;(1R,4R,7S,10R,13S,16R,19S)-7-[(1H-indol-3-yl)methyl]-10-(2-methylpropyl)-4,13,16,19-tetra(propan-2-yl)-21-thia-3,6,9,12,15,18,23-heptaazabicyclo[18.2.1]tricosane-2,5,8,11,14,17-hexone;(1R,4R,7S,10R,13S,16R,19S)-7-(1H-indol-3-ylmethyl)-10-(2-methylpropyl)-4,13,16,19-tetra(propan-2-yl)-21-thia-3,6,9,12,15,18,23-heptazabicyclo[18.2.1]tricosane-2,5,8,11,14,17-hexone;(1R,4R,7S,10R,13S,16R,19S)-7-((1H-indol-3-yl)methyl)-10-(2-methylpropyl)-4,13,16,19-tetra(propan-2-yl)-21-thia-3,6,9,12,15,18,23-heptaazabicyclo(18.2.1)tricosane-2,5,8,11,14,17-hexone;(1R,4R,7S,10R,13S,16R,19S)-7-(1H-indol-3-ylmethyl)-10-(2-methylpropyl)-4,13,16,19-tetra(propan-2-yl)-21-thia-3,6,9,12,15,18,23-heptazabicyclo(18.2.1)tricosane-2,5,8,11,14,17-hexone;CHEMBL4868284;SCHEMBL18102658;DTXSID801336028;EX-A5148;HY-P4200;DA-55065;CS-0647596;Q26156270;
Lugdunin is a novel cyclic peptide antibiotic originally isolated from the bacterium Staphylococcus lugdunensis. Characterized by its unique thiazolidine-containing structure, lugdunin exhibits a distinct mode of action compared to classical antibiotics, positioning it as a valuable subject in the study of antimicrobial peptides. Its emergence has garnered significant attention in biochemical and microbiological research due to its ability to inhibit the growth of multidrug-resistant Gram-positive pathogens. The compound's unusual biosynthetic origin and potent biological activity make it an important tool for probing microbial competition, peptide engineering, and mechanisms of antimicrobial resistance.
Antimicrobial Mechanism Studies: Lugdunin is extensively applied in research focused on elucidating novel mechanisms of antibacterial action. Its cyclic structure and non-canonical amino acid composition provide a model for investigating how structural features influence membrane disruption and bacterial cell death. Researchers utilize the peptide to dissect interactions with bacterial membranes, evaluate the induction of oxidative stress, and assess its impact on essential cellular processes in target organisms. These studies contribute to a deeper understanding of how non-traditional peptides exert bactericidal effects, informing the development of next-generation antimicrobials.
Microbial Competition and Ecological Interactions: The compound is a powerful tool in the study of microbial ecology, particularly in understanding interspecies competition within complex microbial communities. By introducing lugdunin into co-culture assays or microbiome models, scientists can observe its influence on population dynamics, niche colonization, and suppression of pathogenic bacteria. Such research is especially relevant for exploring the natural defense strategies employed by commensal bacteria and their role in maintaining microbial homeostasis on human skin and mucosal surfaces.
Peptide Biosynthesis and Engineering: As a representative of ribosomally synthesized and post-translationally modified peptides (RiPPs), lugdunin serves as a template for biosynthetic pathway analysis and peptide engineering. Investigators employ the compound to dissect the enzymatic steps involved in thiazolidine ring formation and cyclization, offering insights into natural product biosynthesis. Additionally, its structure inspires the design of synthetic analogs and engineered variants with altered activity spectra or improved stability, advancing the field of peptide-based drug discovery and synthetic biology.
Resistance Mechanism Research: Lugdunin is instrumental in probing the molecular basis of bacterial resistance to peptide antibiotics. By exposing bacterial strains to the compound under controlled laboratory conditions, researchers can identify adaptive responses, resistance gene expression, and potential genetic mutations that confer reduced susceptibility. This application aids in anticipating resistance development and supports the rational design of peptide derivatives with minimized resistance potential.
Analytical and Structural Characterization: The unique chemical features of lugdunin make it a prime candidate for advanced analytical and structural studies. Scientists utilize techniques such as nuclear magnetic resonance spectroscopy, mass spectrometry, and X-ray crystallography to characterize its conformation, post-translational modifications, and interactions with biological targets. These investigations not only elucidate the relationship between structure and function but also provide benchmarks for the identification and characterization of other bioactive cyclic peptides in natural product research.
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