KK14(R)

KK14(R) is a Lys-rich peptide variant designed to provide a highly cationic environment along the chain. Positive charges favor interaction with anionic membranes, nucleic acids, or acidic protein surfaces. Researchers analyze its secondary structure and aggregation tendencies in different solvents. Applications include cell-penetrating motif studies, complex coacervate modeling, and charge-driven assembly research.

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

CAT No: R2727

Synonyms/Alias:KK14(R); HY-P10329; CS-1051158.

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M.F/Formula
C96H138N26O14
M.W/Mr.
1880.3
Sequence
One Letter Code:KKFFRAWWAPRFLK
Three Letter Code:H-Lys-Lys-Phe-Phe-Arg-Ala-Trp-Trp-Ala-Pro-Arg-Phe-Leu-Lys-NH2

KK14(R) is a synthetic carbohydrate compound renowned for its unique structural properties and versatility in biochemical research. As a member of the oligosaccharide family, KK14(R) features a carefully engineered configuration that enables specific interactions with various biological molecules. Its stability, solubility in aqueous environments, and compatibility with a range of analytical techniques make it a preferred choice for researchers seeking to explore carbohydrate-mediated processes. The compound's stereochemistry, denoted by the (R) configuration, allows for precise studies of chiral recognition and molecular binding events, facilitating advanced investigations into glycoscience. KK14(R) is frequently utilized in research settings where high specificity and reproducibility are paramount, contributing to a deeper understanding of carbohydrate functions in biological systems.

Glycobiology research: KK14(R) plays a pivotal role in glycobiology research by serving as a model substrate for probing the mechanisms of protein-carbohydrate recognition. Through its defined structure, scientists can investigate the binding affinities and selectivity of lectins, glycosyltransferases, and other carbohydrate-interacting proteins. This enables detailed mapping of glycan recognition patterns, advancing knowledge on cell signaling, immune response modulation, and pathogen-host interactions. The compound's utility in glycan microarray platforms further enhances its value, allowing high-throughput screening of protein-glycan interactions and supporting the development of new diagnostic tools.

Enzyme substrate analysis: As a specialized substrate, KK14(R) is instrumental in the study of carbohydrate-active enzymes, particularly glycosidases and glycosyltransferases. Researchers employ it to assess enzyme specificity, catalytic efficiency, and reaction kinetics under controlled conditions. By monitoring the enzymatic transformation of KK14(R), investigators gain insights into enzyme mechanisms and substrate preferences, facilitating enzyme engineering and the discovery of novel biocatalysts. Its defined stereochemistry is especially beneficial for distinguishing between enzyme isoforms or mutants that exhibit subtle differences in substrate recognition.

Molecular recognition studies: The unique chiral configuration of this carbohydrate compound makes it an excellent tool for exploring molecular recognition phenomena. Scientists utilize KK14(R) to dissect the stereochemical requirements of binding interactions between carbohydrates and their biological partners, such as antibodies, receptors, or small-molecule inhibitors. These studies are essential for understanding the molecular basis of specificity in biological systems, guiding the rational design of carbohydrate-based probes, inhibitors, or mimetics for further research and development.

Biomaterials development: KK14(R) is increasingly incorporated into the design of novel biomaterials, where its carbohydrate moieties impart desirable properties such as biocompatibility, hydration, and molecular recognition. By integrating it into hydrogels, coatings, or scaffolds, researchers can create materials that mimic natural glycan environments, promoting cell adhesion, proliferation, or differentiation. The compound's modular structure allows for chemical modifications, enabling the fine-tuning of material properties for applications in tissue engineering, biosensing, or drug delivery research.

Analytical method validation: In analytical chemistry, KK14(R) serves as a valuable reference standard for the development and validation of carbohydrate detection and quantification methods. Its well-defined structure and consistent behavior under various analytical conditions make it suitable for calibrating instruments and verifying method accuracy. Researchers rely on this compound to optimize protocols for chromatographic separation, mass spectrometry analysis, or capillary electrophoresis, ultimately ensuring reliable and reproducible measurement of carbohydrates in complex biological samples.

In summary, KK14(R) stands out as a multifaceted tool in modern carbohydrate research, supporting advancements in glycobiology, enzymology, molecular recognition, biomaterials science, and analytical chemistry. Its structural precision and adaptability empower researchers to address fundamental questions in glycoscience, develop innovative materials, and refine analytical techniques, underscoring its enduring value in the scientific community.

InChI
InChI=1S/C96H138N26O14/c1-57(2)49-74(88(130)112-70(81(101)123)38-19-22-44-98)117-90(132)76(51-61-29-10-6-11-30-61)119-86(128)73(41-25-47-107-96(104)105)115-93(135)80-42-26-48-122(80)94(136)59(4)111-87(129)78(53-63-55-108-68-36-16-14-33-65(63)68)121-92(134)79(54-64-56-109-69-37-17-15-34-66(64)69)116-82(124)58(3)110-84(126)72(40-24-46-106-95(102)103)114-89(131)75(50-60-27-8-5-9-28-60)120-91(133)77(52-62-31-12-7-13-32-62)118-85(127)71(39-20-23-45-99)113-83(125)67(100)35-18-21-43-97/h5-17,27-34,36-37,55-59,67,70-80,108-109H,18-26,35,38-54,97-100H2,1-4H3,(H2,101,123)(H,110,126)(H,111,129)(H,112,130)(H,113,125)(H,114,131)(H,115,135)(H,116,124)(H,117,132)(H,118,127)(H,119,128)(H,120,133)(H,121,134)(H4,102,103,106)(H4,104,105,107)/t58-,59-,67-,70-,71-,72-,73-,74-,75-,76-,77-,78-,79-,80-/m0/s1
InChI Key
VJHRZHBBVXVBOK-DRNPRWLXSA-N

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