H-Arg-Gly-OH HCl

H-Arg-Gly-OH·HCl provides a basic-neutral dipeptide in a soluble hydrochloride form, ideal for charge-solubility and enzyme-recognition experiments. The guanidinium group participates in strong electrostatic and hydrogen-bond interactions. Researchers examine its role as a minimal trypsin-recognition element. Applications include substrate-fragment studies, folding research, and salt-form comparison.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
H-Arg-Gly-OH HCl(CAS 105241-88-1)

CAT No: R2363

CAS No:105241-88-1

Synonyms/Alias:H-Arg-Gly-OH HCl;105241-88-1;H-Arg-Gly-OH . HCl;2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetic acid;hydrochloride;MFCD00237781;H-Arg-Gly-OH-HCl;H-Arg-Gly-OH.HCl;(S)-2-(2-amino-5-guanidinopentanamido)acetic acid hydrochloride;FA108265;(S)-2-(2-Amino-5-guanidinopentanamido)acetic acid xhydrochloride;

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M.F/Formula
C8H18ClN5O3
M.W/Mr.
267.71
Sequence
One Letter Code:RG
Three Letter Code:H-Arg-Gly-OH.HCl

H-Arg-Gly-OH HCl, also known as L-Arginylglycine hydrochloride, is a synthetic dipeptide composed of arginine and glycine residues, stabilized as its hydrochloride salt. This compound is valued in biochemical research for its defined structure, high solubility in aqueous solutions, and ability to mimic naturally occurring peptide fragments. Its unique combination of a basic guanidinium group from arginine and the small, flexible glycine residue makes it an attractive model for studying peptide interactions, enzymatic processing, and molecular recognition. Researchers often employ H-Arg-Gly-OH HCl to investigate peptide transport mechanisms, substrate specificity of peptidases, and the physicochemical properties of short peptides in various environments. Its versatility and compatibility with a range of analytical techniques further enhance its utility across multiple fields of life sciences.

Peptide Transport Studies: H-Arg-Gly-OH HCl is widely used to probe the mechanisms of peptide uptake and translocation across biological membranes. By incorporating this dipeptide in cellular uptake assays, scientists can analyze the specificity and efficiency of peptide transporters such as PEPT1 and PEPT2. Its defined structure allows for the systematic investigation of how different peptide sequences influence transporter binding and translocation, offering insights into nutrient absorption and drug delivery strategies that leverage peptide carriers.

Enzyme Substrate Characterization: The dipeptide serves as an efficient substrate for evaluating the activity and specificity of various peptidases, including aminopeptidases and dipeptidyl peptidases. Researchers utilize H-Arg-Gly-OH HCl in enzymatic assays to determine cleavage rates, identify substrate recognition motifs, and assess enzyme kinetics. The presence of both a basic and a neutral amino acid residue enables detailed studies on how side-chain properties affect enzyme-substrate interactions, which is critical for designing inhibitors or modifying enzyme selectivity for biotechnological applications.

Protein Interaction Modeling: L-Arginylglycine hydrochloride is frequently employed in structural biology and molecular modeling to simulate protein-peptide interactions. Its simple yet representative structure allows for the exploration of hydrogen bonding, electrostatic interactions, and conformational preferences in peptide-binding domains. By integrating this dipeptide into computational and experimental binding studies, researchers can elucidate the principles governing recognition and affinity between short peptides and protein targets, informing the development of novel ligands or therapeutic peptides.

Peptide Stability and Solubility Analysis: The compound's favorable solubility profile makes it an excellent candidate for examining the stability and aggregation behavior of short peptides in solution. Scientists use H-Arg-Gly-OH HCl as a model system to study the effects of ionic strength, pH, and temperature on peptide solubility and structural integrity. These investigations contribute to a better understanding of peptide formulation, storage, and delivery, particularly in the context of pharmaceutical and biochemical research where peptide stability is a key concern.

Analytical Method Development: In analytical chemistry, H-Arg-Gly-OH HCl is often selected as a standard or reference compound for the calibration and validation of chromatographic and spectroscopic methods. Its consistent behavior under various analytical conditions supports the optimization of protocols for peptide detection, quantification, and purity assessment. The use of this dipeptide in method development ensures accuracy and reproducibility in the analysis of complex peptide mixtures, which is essential for quality control in research and industrial settings.

Biomaterials and Surface Modification: Researchers explore the application of L-Arginylglycine hydrochloride in the design and functionalization of biomaterials. Its incorporation into polymeric matrices or surface coatings imparts bioactive properties, such as enhanced cell adhesion or tailored interaction with biological molecules. By leveraging the chemical versatility of this dipeptide, scientists can develop advanced materials for tissue engineering, biosensing, and regenerative medicine, expanding the potential of peptide-based technologies in material science.

InChI
InChI=1S/C8H17N5O3.ClH/c9-5(2-1-3-12-8(10)11)7(16)13-4-6(14)15;/h5H,1-4,9H2,(H,13,16)(H,14,15)(H4,10,11,12);1H/t5-;/m0./s1
InChI Key
LBJDXUKLQUTBSV-JEDNCBNOSA-N

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