Novexatin (NP213) is a rapidly acting, novel, first-in-class synthetic antimicrobial peptide (AMP), has anti-fungal activities. NP213 targets the fungal cytoplasmic membrane and plays its role via membrane perturbation and disruption. NP213 is effective and well-tolerated in resolving nail fungal infections.
CAT No: R1890
CAS No:942577-31-3
Synonyms/Alias:Novexatin;942577-31-3;NP213;2-[3-[(2S,5S,8S,11S,14S,17S,20S)-5,8,11,14,17,20-hexakis[3-(diaminomethylideneamino)propyl]-3,6,9,12,15,18,21-heptaoxo-1,4,7,10,13,16,19-heptazacyclohenicos-2-yl]propyl]guanidine;CHEMBL2203696;SCHEMBL19712180;EX-A7462;AKOS040764209;DA-76279;HY-126810;CS-0107537;1,1',1'',1''',1'''',1''''',1''''''-(((2S,5S,8S,11S,14S,17S,20S)-3,6,9,12,15,18,21-Heptaoxo-1,4,7,10,13,16,19-heptaazacyclohenicosane-2,5,8,11,14,17,20-heptayl)heptakis(propane-3,1-diyl))heptaguanidine;
Chemical Name:2-[3-[(2S,5S,8S,11S,14S,17S,20S)-5,8,11,14,17,20-hexakis[3-(diaminomethylideneamino)propyl]-3,6,9,12,15,18,21-heptaoxo-1,4,7,10,13,16,19-heptazacyclohenicos-2-yl]propyl]guanidine
Novexatin (NP213) is a synthetic peptide compound engineered for its unique biochemical properties, notably its cationic amphipathic structure that facilitates strong interactions with biological membranes. As a member of the antifungal peptide class, it is distinguished by a sequence derived from naturally occurring host-defense peptides, optimized for stability and activity in challenging environments. Its design enables it to mimic innate immune system mechanisms, making it particularly relevant for research into antimicrobial strategies and membrane-active peptide functionalities. The compound's physicochemical characteristics, including resistance to proteolytic degradation and a defined mechanism of membrane disruption, have established it as a valuable tool in the study of peptide-membrane interactions and the development of novel antimicrobial agents.
Antimicrobial research: NP213 is widely utilized in studies investigating peptide-based antimicrobial mechanisms, particularly against fungal pathogens. Its ability to disrupt fungal cell membranes without relying on traditional enzymatic pathways provides a model system for elucidating the structure-activity relationships of cationic peptides. Researchers leverage its well-characterized activity to probe how sequence modifications affect selectivity and potency, advancing the understanding of next-generation antimicrobial strategies that bypass conventional resistance mechanisms.
Membrane interaction studies: The amphipathic nature of this peptide makes it an ideal probe for examining peptide-lipid interactions and membrane permeability. Experimental models employing NP213 help clarify the biophysical principles underlying peptide-induced membrane destabilization, pore formation, and selective targeting of microbial versus mammalian membranes. Such studies inform the rational design of membrane-active agents and contribute to the broader field of peptide-membrane biophysics.
Peptide stability evaluation: NP213's engineered resistance to proteolytic enzymes positions it as a reference compound in research focused on peptide stability and degradation pathways. By comparing its stability profile to other antimicrobial peptides, scientists can identify sequence features and structural motifs that confer enhanced durability in biological matrices. These insights are instrumental for designing peptides with improved pharmacokinetic properties for research use.
Peptide synthesis optimization: The synthetic accessibility and structural features of NP213 make it a valuable standard in the development and validation of solid-phase peptide synthesis protocols. Its sequence complexity and amphipathic character challenge synthesis workflows, providing a robust benchmark for evaluating coupling efficiencies, purification strategies, and analytical characterization methods. Such applications support the advancement of reliable manufacturing techniques for research peptides.
Antifungal mechanism elucidation: Due to its well-defined mode of action, NP213 serves as a model compound for dissecting the molecular basis of antifungal activity in peptide-based agents. Research employing this peptide enables detailed investigations into how cationic peptides interact with fungal cell components, disrupt membrane integrity, and trigger downstream cellular responses. These mechanistic studies are fundamental for guiding the rational development of novel antifungal peptides and for understanding resistance phenomena in pathogenic fungi.
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