KSL 128114

KSL 128114 is a designed cationic peptide with alternating hydrophobic and lysine residues that encourage amphipathic helix formation. Such topology promotes interaction with bacterial-mimetic membranes in vitro. Researchers investigate its folding, aggregation, and surface-disruption properties. Applications include antimicrobial-peptide modeling, membrane-activity profiling, and sequence optimization.

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

CAT No: R2806

Synonyms/Alias:HY-P10331;KSL 128114

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M.F/Formula
C96H165N39O21
M.W/Mr.
2201.6
Sequence
One Letter Code:RRRGRKKRRSHWXXDI
Three Letter Code:Ac-D-Arg-Arg-D-Arg-Gly-D-Arg-Lys-D-Lys-Arg-D-Arg-Ser-His-Trp-Gly(tBu)-Chg-Asp-Ile-OH

KSL 128114 is a synthetic peptide compound recognized for its distinctive sequence and structural properties, making it a valuable tool in contemporary biochemical research. As a member of the peptide family, it consists of a specific arrangement of amino acids designed to confer targeted biological activity and molecular recognition capabilities. Its utility stems from the ability to interact with various biomolecules, enabling researchers to probe protein-protein interactions, study cell signaling pathways, and develop novel assay systems. The molecular design of KSL 128114 allows for precise modulation of its physicochemical characteristics, which supports its integration into a wide range of experimental protocols. Its relevance extends across disciplines such as molecular biology, pharmacology, and peptide engineering, where synthetic peptides are critical for advancing both fundamental and applied research.

Peptide interaction studies: KSL 128114 serves as a robust model for investigating peptide-mediated interactions with proteins, nucleic acids, or cellular membranes. By leveraging its defined sequence, researchers can dissect binding affinities, map interaction sites, and elucidate the structural determinants governing molecular recognition. Such studies provide insights into the mechanisms underlying signal transduction, cellular communication, and macromolecular assembly, ultimately advancing the understanding of complex biological systems.

Peptide synthesis optimization: In the context of synthetic methodology development, KSL 128114 is frequently employed as a test substrate for evaluating solid-phase peptide synthesis (SPPS) protocols and purification strategies. Its defined sequence and physicochemical profile make it an ideal candidate for benchmarking coupling efficiencies, resin compatibility, and chromatographic separation techniques. These optimization studies contribute to improved yields, purity, and scalability in peptide manufacturing, supporting both research and industrial peptide production.

Assay development: The unique properties of KSL 128114 facilitate its use in the design and validation of bioanalytical assays, such as enzyme-linked immunosorbent assays (ELISA), fluorescence polarization assays, or surface plasmon resonance (SPR) platforms. By incorporating this peptide as a standard, reference, or probe, scientists can establish assay sensitivity, specificity, and reproducibility. Its inclusion ensures consistent performance in high-throughput screening and mechanistic studies, which are essential for drug discovery and biomarker validation efforts.

Structure-activity relationship (SAR) analysis: KSL 128114 is instrumental in systematic SAR investigations aimed at correlating specific sequence motifs or modifications with biological activity. Through targeted substitutions, truncations, or chemical modifications, researchers can delineate the functional domains responsible for activity, stability, or selectivity. These SAR studies inform the rational design of next-generation peptides with enhanced properties, supporting innovation in peptide therapeutics, diagnostics, and molecular probes.

Cellular uptake and delivery research: The peptide is also utilized in exploring mechanisms of cellular internalization and delivery, particularly in studies focused on peptide-mediated transport across biological membranes. By conjugating KSL 128114 to fluorophores, nanoparticles, or bioactive cargos, investigators can monitor uptake efficiency, trafficking pathways, and intracellular localization. Such research advances the development of peptide-based delivery systems for biomolecules, expanding the toolkit for intracellular targeting and molecular imaging applications.

InChI
InChI=1S/C96H165N39O21/c1-7-51(2)72(89(155)156)133-84(150)68(45-71(139)140)131-87(153)73(53-23-9-8-10-24-53)134-88(154)74(96(4,5)6)135-85(151)66(43-54-46-118-57-26-12-11-25-56(54)57)129-83(149)67(44-55-47-111-50-120-55)130-86(152)69(49-136)132-82(148)65(34-22-42-117-95(109)110)128-81(147)64(33-21-41-116-94(107)108)127-79(145)62(28-14-16-36-98)125-78(144)61(27-13-15-35-97)124-77(143)60(31-19-39-114-92(103)104)122-70(138)48-119-75(141)58(29-17-37-112-90(99)100)123-80(146)63(32-20-40-115-93(105)106)126-76(142)59(121-52(3)137)30-18-38-113-91(101)102/h11-12,25-26,46-47,50-51,53,58-69,72-74,118,136H,7-10,13-24,27-45,48-49,97-98H2,1-6H3,(H,111,120)(H,119,141)(H,121,137)(H,122,138)(H,123,146)(H,124,143)(H,125,144)(H,126,142)(H,127,145)(H,128,147)(H,129,149)(H,130,152)(H,131,153)(H,132,148)(H,133,150)(H,134,154)(H,135,151)(H,139,140)(H,155,156)(H4,99,100,112)(H4,101,102,113)(H4,103,104,114)(H4,105,106,115)(H4,107,108,116)(H4,109,110,117)/t51-,58+,59+,60+,61-,62+,63-,64-,65+,66-,67-,68-,69-,72-,73-,74+/m0/s1
InChI Key
JHIMDMTVBCBWIO-UJEPQUICSA-N

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