Pexiganan acetate

Pexiganan acetate is a short chain synthetic cationic peptides. It is being studied as potential antimicrobial agents. These peptides are found widely in nature in mammals, fish, insecs and amphibians.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: 10-101-182

CAS No:172820-23-4

Synonyms/Alias:Pexiganan acetate;172820-23-4;Cytolex;UNII-63S35FF5KS;NS00121075;

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cGMP Peptide
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M.F/Formula
C124H214N32O24
M.W/Mr.
2537.2
Sequence
One Letter Code:GIGKFLKKAKKFGKAFVKLLKK
Three Letter Code:H-Gly-Ile-Gly-Lys-Phe-Leu-Lys-Lys-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Lys-Leu-Leu-Lys-Lys-NH2.CH3CO2H
Application
Antibacterial.
Appearance
White or off-white lyophilized powder
Purity
>98 %
Areas of Interest
Diabetic foot ulcer

Pexiganan acetate is a synthetic peptide derivative modeled after magainin, an antimicrobial peptide originally isolated from the skin of the African clawed frog, Xenopus laevis. As a cationic, amphipathic peptide, it exhibits potent activity against a broad spectrum of Gram-positive and Gram-negative bacteria, making it a valuable tool for researchers investigating host defense mechanisms and peptide-based antimicrobial strategies. Its well-characterized structure, stability, and membrane-disruptive properties have positioned it as a reference compound in the study of antimicrobial peptides (AMPs), membrane biology, and peptide engineering. The relevance of pexiganan acetate extends across microbiology, biochemistry, pharmacology, and peptide research, providing a robust platform for exploring both fundamental and applied aspects of peptide function.

Antimicrobial research: Pexiganan acetate is widely utilized as a model AMP for evaluating the mechanisms of peptide-induced bacterial cell death. Its ability to disrupt microbial membranes through pore formation or membrane destabilization allows researchers to dissect the physicochemical parameters that govern peptide-membrane interactions. Studies employing this compound aid in elucidating the structural motifs and charge distributions critical for selective bactericidal activity, thereby informing the design of next-generation antimicrobial agents.

Peptide structure-activity relationship studies: The defined sequence and modifiable structure of pexiganan acetate make it an ideal candidate for systematic investigations into the relationship between peptide primary structure and biological function. By introducing targeted mutations or chemical modifications, researchers can assess the impact of sequence changes on antimicrobial potency, selectivity, and stability. These studies contribute to the broader understanding of how peptide conformation, amphipathicity, and charge influence biological activity, supporting rational peptide design.

Membrane biophysics: Owing to its robust membrane-disruptive capabilities, pexiganan acetate serves as a valuable probe in biophysical studies of lipid bilayer integrity and dynamics. Researchers employ it to investigate the biophysical responses of model membranes, such as liposomes or supported lipid bilayers, to peptide-induced perturbations. Such experiments provide mechanistic insights into the modes of action of AMPs and help identify factors that modulate membrane susceptibility, such as lipid composition, membrane curvature, and surface charge.

Antimicrobial resistance research: The increasing prevalence of multidrug-resistant bacteria has prompted interest in alternative antimicrobial strategies. Pexiganan acetate is frequently used in laboratory settings to assess bacterial resistance development under selective pressure from peptide-based agents. By monitoring adaptive responses, such as changes in membrane composition or efflux mechanisms, researchers can identify potential resistance pathways and evaluate the evolutionary robustness of peptide antibiotics, thereby informing the development of more durable antimicrobial therapies.

Peptide formulation and delivery studies: The amphipathic and cationic nature of pexiganan acetate also renders it useful in the exploration of peptide formulation, encapsulation, and controlled delivery systems. Researchers investigate its compatibility with various carrier matrices, such as hydrogels, nanoparticles, or polymeric films, to optimize stability and release profiles. These studies facilitate the advancement of peptide delivery technologies, supporting the broader application of AMPs in research and industrial contexts where controlled antimicrobial activity is desired.

Source#
Synthetic
Shipping Condition
Shipped at room temperature
InChI
InChI=1S/C122H210N32O22.C2H4O2/c1-13-78(10)103(153-99(155)71-132)121(175)135-73-101(157)139-86(49-25-34-58-125)110(164)152-97(69-82-43-19-15-20-44-82)119(173)150-94(66-75(4)5)117(171)145-90(53-29-38-62-129)113(167)142-87(50-26-35-59-126)109(163)137-79(11)105(159)141-88(51-27-36-60-127)112(166)143-91(54-30-39-63-130)114(168)151-96(68-81-41-17-14-18-42-81)107(161)134-72-100(156)138-85(48-24-33-57-124)108(162)136-80(12)106(160)147-98(70-83-45-21-16-22-46-83)120(174)154-102(77(8)9)122(176)146-92(55-31-40-64-131)115(169)148-95(67-76(6)7)118(172)149-93(65-74(2)3)116(170)144-89(52-28-37-61-128)111(165)140-84(104(133)158)47-23-32-56-123;1-2(3)4/h14-22,41-46,74-80,84-98,102-103H,13,23-40,47-73,123-132H2,1-12H3,(H2,133,158)(H,134,161)(H,135,175)(H,136,162)(H,137,163)(H,138,156)(H,139,157)(H,140,165)(H,141,159)(H,142,167)(H,143,166)(H,144,170)(H,145,171)(H,146,176)(H,147,160)(H,148,169)(H,149,172)(H,150,173)(H,151,168)(H,152,164)(H,153,155)(H,154,174);1H3,(H,3,4)/t78-,79-,80-,84-,85-,86-,87-,88-,89-,90-,91-,92-,93-,94-,95-,96-,97-,98-,102-,103-;/m0./s1
InChI Key
PAYZGDCWKMPDRW-ITJSRVBASA-N
Canonical SMILES
CCC(C)C(C(=O)NCC(=O)NC(CCCCN)C(=O)NC(CC1=CC=CC=C1)C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)NC(CCCCN)C(=O)NC(C)C(=O)NC(CCCCN)C(=O)NC(CCCCN)C(=O)NC(CC2=CC=CC=C2)C(=O)NCC(=O)NC(CCCCN)C(=O)NC(C)C(=O)NC(CC3=CC=CC=C3)C(=O)NC(C(C)C)C(=O)NC(CCCCN)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(CCCCN)C(=O)NC(CCCCN)C(=O)N)NC(=O)CN.CC(=O)O
Isomeric SMILES
CC[C@H](C)[C@@H](C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC2=CC=CC=C2)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC3=CC=CC=C3)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N)NC(=O)CN.CC(=O)O

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