H-D-Leu-Thr-Arg-PNA

This sequence of amino acids would be translated as: Histidine-Aspartic Acid-Leucine-Threonine-Arginine-Pseudonucleic Acid.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
H-D-Leu-Thr-Arg-PNA(CAS 122630-72-2)

CAT No: 10-101-241

CAS No:122630-72-2

Synonyms/Alias:H-D-Leu-Thr-Arg-pNA;122630-72-2;D-Leu-Thr-Arg-pNA;H-D-Leu-Thr-Arg-pNA acetate salt;(2R)-2-Amino-N-[(2S,3R)-1-[[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]-4-methylpentanamide;D-Leucyl-L-threonyl-N-(4-nitrophenyl)-L-argininamide;HY-P4462;DA-53908;FL110734;CS-0654354;

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cGMP Peptide
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M.F/Formula
C22H36N8O6
M.W/Mr.
508.6
Sequence
One Letter Code:LTR
Three Letter Code:H-D-Leu-Thr-Arg-pNA

H-D-Leu-Thr-Arg-PNA is a synthetic peptide nucleic acid (PNA) conjugate designed to combine the unique structural features of peptide backbones with the nucleic acid recognition properties of PNAs. As a hybrid molecule, it incorporates the amino acid sequence D-Leucine-Threonine-Arginine linked to a PNA moiety, offering enhanced stability and specificity in molecular recognition applications. Its chimeric architecture enables researchers to exploit both the biochemical versatility of peptides and the robust hybridization capabilities of PNAs, making it a valuable tool in advanced molecular biology and biochemistry research. H-D-Leu-Thr-Arg-PNA is particularly well-suited for studies requiring high-affinity binding to complementary nucleic acid sequences, as well as for investigations into peptide-mediated cellular delivery mechanisms and biomolecular interactions.

Molecular recognition studies: The unique combination of peptide and PNA components allows this conjugate to serve as a highly specific probe for nucleic acid detection and hybridization assays. Its PNA backbone exhibits strong affinity and selectivity for DNA or RNA targets due to the absence of charged phosphate groups, reducing electrostatic repulsion and increasing binding stability. Researchers utilize such constructs to investigate sequence-specific interactions, elucidate binding kinetics, and develop novel nucleic acid detection platforms for fundamental genomics and transcriptomics research.

Antisense and gene regulation research: H-D-Leu-Thr-Arg-PNA is often employed in studies aiming to modulate gene expression at the transcriptional or translational level. The PNA segment is capable of forming stable duplexes with complementary RNA or DNA sequences, thereby sterically blocking transcription or translation processes. The attached peptide sequence can be tailored to enhance cellular uptake or nuclear localization, providing a versatile scaffold for exploring gene knockdown strategies, antisense inhibition mechanisms, and the development of gene-silencing tools in vitro.

Peptide-mediated delivery investigations: The presence of D-Leucine, Threonine, and Arginine residues in the peptide portion is strategically chosen to facilitate cellular uptake and endosomal escape. Researchers leverage this property to study the translocation efficiency of PNA conjugates across cellular membranes. Such studies are critical for optimizing peptide-based delivery vectors and understanding the parameters that govern intracellular trafficking, thus advancing the design of next-generation molecular delivery systems for research applications.

Protein-nucleic acid interaction analysis: The hybrid structure of this compound enables detailed exploration of protein-nucleic acid interactions, particularly in the context of sequence recognition and binding specificity. By serving as a model substrate, it aids in dissecting the molecular determinants of peptide-nucleic acid association, informing the design of synthetic analogs for biophysical studies. These insights are essential for the rational development of new molecular probes and the characterization of protein-DNA/RNA interfaces.

Analytical and diagnostic tool development: The robust hybridization properties and enhanced stability of H-D-Leu-Thr-Arg-PNA make it an attractive candidate for the development of analytical assays and diagnostic platforms. Its resistance to enzymatic degradation, combined with sequence-specific binding, allows for the creation of highly sensitive detection systems for nucleic acid targets in complex biological samples. Researchers utilize these features to design innovative biosensors, microarray probes, and other analytical tools that require reliable and reproducible performance in demanding research environments.

Shipping Condition
Room temperature in continental US; may vary elsewhere.
InChI
InChI=1S/C22H36N8O6/c1-12(2)11-16(23)19(32)29-18(13(3)31)21(34)28-17(5-4-10-26-22(24)25)20(33)27-14-6-8-15(9-7-14)30(35)36/h6-9,12-13,16-18,31H,4-5,10-11,23H2,1-3H3,(H,27,33)(H,28,34)(H,29,32)(H4,24,25,26)/t13-,16-,17+,18+/m1/s1
InChI Key
IBFUBQKPPLZOLE-ZSGPHXLJSA-N

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