Bactenecin is a cysteine-rich antimicrobial peptide forming stable disulfide-linked structures. Researchers employ it to explore β-sheet stabilization, membrane interaction, and redox behavior. The sequence supports examination of peptide folding in hydrophobic environments. Its unusual architecture allows detailed structural mapping.
CAT No: R2287
CAS No:116229-36-8
Synonyms/Alias:Bactenecin;116229-36-8;Arg-leu-cyclo(cys-arg-ile-val-val-ile-arg-val-cys)-arg;Bactenecin, bovine;Bac7;CHEBI:201834;2-[[28-[[2-[[2-amino-5-(diaminomethylideneamino)pentanoyl]amino]-4-methylpentanoyl]amino]-13,22-di(butan-2-yl)-10,25-bis[3-(diaminomethylideneamino)propyl]-6,9,12,15,18,21,24,27-octaoxo-7,16,19-tri(propan-2-yl)-1,2-dithia-5,8,11,14,17,20,23,26-octazacyclononacosane-4-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic acid;DA-61475;PD150815;
Bactenecin, also known as Bac7, is a cationic antimicrobial peptide originally isolated from bovine neutrophils. This peptide is characterized by its rich content of arginine and proline residues, which contribute to its unique structure and remarkable stability. As a member of the host-defense peptide family, Bactenecin exhibits a broad spectrum of activity against various microorganisms, making it a subject of significant interest in the fields of microbiology, immunology, and peptide-based research. Its ability to interact with microbial membranes and modulate immune responses positions it as a valuable tool for investigating innate immunity and developing novel antimicrobial strategies. Researchers favor Bactenecin for its robust resistance to proteolytic degradation and its potential to serve as a template for the design of new synthetic peptides with enhanced biological activity.
Antimicrobial research: Bactenecin is extensively used in studies aiming to elucidate the mechanisms underlying innate immune responses to bacterial pathogens. By incorporating Bac7 into in vitro and in vivo experiments, researchers can assess its bactericidal properties, membrane-disrupting capabilities, and selectivity toward Gram-negative and Gram-positive bacteria. These investigations help clarify how cationic peptides compromise microbial integrity, offering insights into the development of new antimicrobial agents that bypass conventional resistance mechanisms. Moreover, Bactenecin's ability to interact with lipopolysaccharides and other bacterial surface components supports its use as a model compound for studying peptide-membrane interactions at the molecular level.
Immunomodulation studies: Bac7 plays a pivotal role in research focused on the modulation of host immune responses. Scientists utilize this peptide to explore how endogenous antimicrobial peptides influence cytokine production, leukocyte recruitment, and the activation of various signaling pathways involved in inflammation and pathogen clearance. By examining Bactenecin's effects on immune cell function, researchers gain a deeper understanding of the peptide's dual role in both direct microbial killing and the orchestration of host defense mechanisms. These findings contribute to the broader field of immunology, where host-defense peptides are increasingly recognized as key regulators of immune homeostasis.
Peptide engineering and design: The unique structural features of Bactenecin make it an attractive scaffold for the rational design of synthetic antimicrobial peptides. Researchers leverage its arginine-proline-rich sequence to create analogs with improved stability, selectivity, and potency. By introducing targeted modifications, scientists can optimize peptide-membrane interactions or enhance resistance to enzymatic degradation. Bactenecin thus serves as a blueprint for developing next-generation peptides with tailored biological activities, supporting the advancement of peptide therapeutics and biomaterials.
Biofilm inhibition: Bac7 has been investigated for its capacity to prevent or disrupt bacterial biofilms, which are often resistant to traditional antimicrobial agents. In laboratory settings, the peptide is applied to surfaces or incorporated into coatings to assess its efficacy in inhibiting biofilm formation and promoting the eradication of established biofilms. These studies are crucial for addressing persistent infections associated with medical devices and industrial equipment, where biofilm-associated bacteria pose significant challenges. The ability of Bactenecin to penetrate biofilm matrices and target sessile cells underscores its utility in anti-biofilm research and technology development.
Antifungal and antiviral exploration: Beyond its antibacterial activity, Bactenecin is also evaluated for its effects against fungal and viral pathogens. Researchers investigate its mechanism of action against various fungal species, focusing on membrane disruption and interference with key cellular processes. Additionally, preliminary studies examine its potential to inhibit viral replication or modulate host responses to viral infection. These diverse applications highlight the broad-spectrum potential of Bac7 and stimulate further research into its multifunctional properties, paving the way for innovative strategies to combat a wide range of infectious agents.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More