δ-Hemolysin features a small, amphipathic peptide that readily adopts helical conformations in lipid-mimetic systems. Hydrophobic residues drive membrane association, while polar units fine-tune structural transitions. Researchers examine its dynamic behavior and binding interactions. Use spans natural-toxin modeling, biophysical studies, and membrane-active peptide research.
CAT No: R2518
CAS No:74838-20-3
Synonyms/Alias:delta-Hemolysin;delta-Lysin;Hld protein;Staph delta-hemolysin;delta-Hemolysin, staph aureus;Staphylococcal delta-haemolysin;Hld protein, Staphylococcus aureus;delta Hemolysin, staphylococcus aureus;Delta hemolysin protein, Staphylococcus aureus;74838-20-3;delta-Hemolysin (Staphylococcus aureus strain 186X);DA-52429;
Delta-Hemolysin is a peptide toxin produced by certain strains of Staphylococcus bacteria, recognized for its amphipathic alpha-helical structure and potent surfactant properties. As a member of the phenol-soluble modulin (PSM) family, this small, hydrophobic peptide plays a critical role in bacterial physiology and pathogenesis by disrupting cellular membranes and facilitating the lysis of erythrocytes and other cell types. Its unique biophysical characteristics and involvement in microbial competition, virulence, and immune evasion have made delta-hemolysin a subject of significant interest in microbiology, membrane biochemistry, and host-pathogen interaction research.
Membrane Disruption Studies: Delta-hemolysin is widely utilized as a model peptide for investigating the mechanisms of membrane permeabilization and lytic activity. Its ability to integrate into phospholipid bilayers and induce pore formation enables researchers to dissect the physicochemical principles underlying peptide-induced membrane destabilization. These studies provide valuable insights into the broader class of amphipathic peptides and their relevance to antimicrobial action, innate immunity, and the structural determinants of cytolytic activity.
Host-Pathogen Interaction Research: The peptide serves as a key tool for elucidating the molecular strategies employed by Staphylococcus species during infection. By simulating the effects of bacterial toxins on host cells, delta-hemolysin enables the assessment of immune cell responses, cellular signaling events, and the role of cytolysins in immune evasion. Experimental use of this compound facilitates the identification of host factors involved in toxin susceptibility and the delineation of bacterial virulence pathways.
Peptide Structure-Activity Relationship Analysis: Delta-hemolysin's well-defined sequence and secondary structure make it an ideal candidate for structure-activity relationship (SAR) studies. Researchers employ synthetic analogs and site-directed mutagenesis to probe the relationship between amino acid composition, helical propensity, and biological function. These investigations support the rational design of novel peptides with tailored lytic or antimicrobial properties and contribute to the broader understanding of peptide-membrane interactions.
Antimicrobial Peptide Research: Owing to its natural role as a bacterial defense molecule, delta-hemolysin is frequently studied alongside other antimicrobial peptides to characterize its spectrum of activity, mechanism of action, and synergy with host or microbial factors. Comparative analyses help delineate the evolutionary adaptations of staphylococcal peptides and inform the development of new biomimetic agents for research applications in microbial ecology and synthetic biology.
Analytical Method Development: The peptide's distinct physicochemical properties, including its amphipathicity and membrane-targeting activity, make it useful as a reference compound or positive control in analytical assays. It is employed in the validation of hemolytic activity assays, peptide quantification protocols, and membrane interaction studies, supporting the standardization and optimization of experimental methodologies in peptide biochemistry and microbiological research.
2. The spatiotemporal control of signalling and trafficking of the GLP-1R
4. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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