H-beta-HAsp-OH*HCl

H-beta-HAsp-OH*HCl is a hydrochloride salt form of an H-β-substituted aspartic acid derivative, presented as an amino acid building block with a free carboxylic acid functionality and an amine-bearing N-terminus. The β-amino acid framework incorporates the stereogenic character associated with β-substitution, while the salt form improves handling by pairing the basic site with chloride to support reproducible coupling and downstream salt-compatible workflows. The molecule's primary functional groups enable amide bond formation through standard peptide coupling chemistry, and the carboxylate can participate in selective derivatization to install C-terminal protecting groups or activate for chain extension. The overall structure is well suited to chiral amino acid intermediate preparation and to controlled incorporation of β-functionalized aspartate motifs into peptide-like scaffolds.

1. Peptide Synthesis

H-beta-HAsp-OH*HCl is used in peptide synthesis as a chiral amino acid building block for constructing β-substituted aspartate segments in linear peptides and protected peptide fragments. The presence of an N-terminus and a carboxylic acid allows conversion into an N-protected amino acid derivative and a C-terminal protected form, supporting peptide coupling via carbodiimide or uronium-type activation strategies after appropriate salt neutralization. The β-substitution can influence conformational preferences and side-chain orientation, which is relevant for assembling peptide analogs that probe backbone stereochemistry and local geometry. The hydrochloride counterion can be managed during protection and coupling sequences to maintain reproducible reactivity across batch syntheses, supporting both research-grade peptide construction and process-oriented intermediate preparation.

2. Amino Acid Derivatization

H-beta-HAsp-OH*HCl is applied in amino acid derivatization workflows to generate functionalized aspartate derivatives for downstream synthetic transformations. The free carboxylic acid can be esterified or converted to amide-linked derivatives, enabling C-terminal modification for library synthesis, solubility tuning, or incorporation into larger molecules. The β-substituted stereocenter and amino functionality can be leveraged to access stereodefined intermediates for subsequent side-chain functionalization, including transformations that install additional electrophilic or nucleophilic handles. The salt form supports reproducible handling in fine chemical synthesis, where consistent salt-to-free-base conversion and protection-group installation are key to reliable intermediate generation.

3. Peptidomimetics Construction

H-beta-HAsp-OH*HCl is suitable for peptidomimetic construction in medicinal chemistry research, where β-substituted aspartate motifs can be used to modulate peptide-like recognition. The amino acid backbone provides a defined stereochemical element that can be carried into constrained analogs after N- and C-terminal protection strategies, including conversion to protected building blocks for iterative coupling. The carboxyl functionality supports formation of amide, ester, or other bioisostere-linked linkages that can be used to tune polarity and hydrogen-bonding patterns in SAR studies. The resulting β-functionalized scaffolds can serve as intermediates toward non-natural peptide analogs and structure-defined molecular probes, aligning amino acid chemistry with peptidomimetic synthesis needs.

4. Chemical Biology Probes

H-beta-HAsp-OH*HCl is employed in chemical biology to prepare stereochemically defined amino acid-containing probes for studying biomolecular interactions. The N- and C-functional groups enable attachment to affinity tags, linkers, or reporter-bearing moieties through controlled amide coupling after appropriate protection-group management. The β-substituted aspartate motif can influence binding orientation and local conformational constraints, supporting design of probes that discriminate among structural states in protein-ligand or protein-peptide recognition assays. The hydrochloride salt form can facilitate consistent reagent preparation for conjugation-ready intermediate synthesis, supporting reproducible probe generation for biochemical research.

5. Pharmaceutical Manufacturing Intermediates

H-beta-HAsp-OH*HCl is used as a manufacturing-relevant amino acid intermediate for producing protected β-substituted aspartate derivatives that feed into peptide-based API intermediates and related fine chemicals. The carboxylic acid and amine functionalities enable conversion into industry-compatible protected forms, such as N-protected amino acid derivatives and C-terminal protected intermediates, which are commonly required for controlled peptide coupling in multistep syntheses. The stereochemical integrity associated with the β-substituted center supports route design where epimerization control and protecting-group strategy are central to maintaining specification during scale-up. The salt form supports stable weighing and handling in chemical manufacturing workflows, enabling downstream conversion into coupling-ready intermediates for consistent batch production of amino acid-derived products.

1. A possible role of tachykinin-related peptide on an immune system activity of mealworm beetle, Tenebrio molitor L

2. Oleic acid and glucose regulate glucagon-like peptide 1 receptor expression in a rat pancreatic ductal cell line

3. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis

4. Extended exenatide administration enhances lipid metabolism and exacerbates pancreatic injury in mice on a high fat, high carbohydrate diet

5. Uncarboxylated osteocalcin decreases insulin-stimulated glucose uptake without affecting insulin signaling and regulators of mitochondrial biogenesis in myotubes