LfcinB 17-28 TFA represents a cationic segment of bovine lactoferricin enriched in aromatic and basic residues. The peptide adopts an amphipathic geometry that enhances membrane affinity and folding stability. Researchers analyze its structural transitions in lipid mimetics. Applications include antimicrobial-peptide characterization, membrane-interface studies, and sequence-activity correlation.
CAT No: R2798
LfcinB 17-28 TFA is a synthetic peptide fragment derived from the bovine lactoferricin sequence, specifically corresponding to residues 17 through 28. This peptide is recognized for its cationic and amphipathic properties, which contribute to its ability to interact with biological membranes and influence a range of cellular processes. As a research tool, LfcinB 17-28 TFA is of significant interest in the study of host defense peptides, antimicrobial mechanisms, and peptide-membrane interactions. Its defined sequence and structural features make it a valuable model for investigating the functional domains of lactoferricin and related bioactive peptides.
Antimicrobial research: The peptide fragment is widely utilized as a model system for elucidating the mechanisms underlying peptide-mediated antimicrobial activity. Its sequence, derived from a core region of bovine lactoferricin, enables researchers to study how cationic peptides interact with bacterial membranes, disrupt membrane integrity, and exert bactericidal effects in vitro. By enabling structure-activity relationship studies, LfcinB 17-28 TFA supports the design and evaluation of novel antimicrobial agents and contributes to a deeper understanding of innate immune defense strategies.
Membrane interaction studies: Due to its amphipathic structure, the peptide serves as an effective probe for examining peptide-lipid interactions, membrane permeabilization, and membrane selectivity. Researchers employ this fragment in biophysical assays, such as fluorescence spectroscopy and circular dichroism, to investigate how specific amino acid sequences influence membrane binding and destabilization. These studies provide insights into the determinants of selectivity toward microbial versus mammalian cell membranes, informing the rational design of membrane-active peptides.
Peptide engineering and design: LfcinB 17-28 TFA is frequently used as a template in peptide engineering efforts aimed at optimizing biological activity or stability. By introducing targeted modifications to its sequence or structure, scientists can assess the impact on antimicrobial potency, protease resistance, or other functional properties. This approach supports the development of synthetic analogs with enhanced performance for research applications, as well as the exploration of sequence motifs critical for activity.
Cell signaling and immunomodulation research: Investigations into the immunomodulatory properties of lactoferricin-derived peptides often employ this fragment to assess its influence on cellular responses, cytokine production, or chemotactic activity. Studies utilizing LfcinB 17-28 TFA help clarify how short cationic peptides can modulate immune cell behavior, providing a platform for dissecting the molecular mechanisms of innate immunity and peptide-induced signaling pathways.
Analytical and assay development: The defined sequence and physicochemical properties of LfcinB 17-28 TFA make it a suitable standard or control in a variety of analytical and bioassay formats. Researchers incorporate the peptide into antimicrobial susceptibility assays, peptide quantification protocols, and membrane translocation studies to establish baseline activity or to calibrate experimental systems. Its consistent performance and well-characterized behavior support reproducibility and reliability in peptide-focused research workflows.
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