H-alpha-Me-D-Asp-OH

H-alpha-Me-D-Asp-OH is a D-configured amino acid derivative featuring an α-methyl substituent on the backbone and a free carboxylic acid, with the side chain corresponding to the β-carboxylate of Asp. The additional α-methyl stereocenter increases steric differentiation around the amino acid nitrogen and carboxylate, which can influence peptide coupling rates, conformational preferences, and protection-group behavior. The molecule contains a primary amino functionality and two carboxyl groups in a form that can be selectively protected or activated for downstream peptide bond formation and carboxylate derivatization. As a chiral amino acid building block and intermediate, H-alpha-Me-D-Asp-OH can be used to introduce stereochemically defined, sterically biased Asp analogs into peptides and peptidomimetics, while also serving as a precursor for functional group transformations relevant to synthetic organic chemistry and biochemical research.

1. Peptide Synthesis

H-alpha-Me-D-Asp-OH is applied in peptide synthesis where D-configuration and the α-methyl group enable incorporation of sterically constrained Asp residues into linear peptides and constrained analogs. The amino acid backbone supports standard peptide coupling chemistry after appropriate N-protection, while the side-chain β-carboxylic acid can be orthogonally protected to allow selective activation for sequential chain assembly. The presence of two carboxyl groups supports controlled C-terminal versus side-chain functionalization strategies, including formation of side-chain amides or esters depending on orthogonal protection choices. Downstream peptide products can be used as reference scaffolds for conformational studies and as building blocks for generating libraries of Asp-containing peptidomimetics.

2. Peptidomimetics And SAR Studies

H-alpha-Me-D-Asp-OH is utilized in peptidomimetic construction and structure-activity relationship studies to probe how α-methyl substitution alters local geometry, hydrogen-bonding patterns, and backbone flexibility relative to canonical D-Asp. The chiral α-methyl substituent can bias conformations and modulate the spatial presentation of the side-chain carboxyl group, which is often a key recognition element in receptor- and enzyme-binding motifs. Selective protection of the amino and carboxyl functionalities enables systematic generation of analog series with controlled stereochemistry and side-chain derivatization. Synthesized derivatives can then be used as chemically defined inputs for SAR workflows, enabling structure-informed comparisons across Asp analogs.

3. Chemical Biology Labeling

H-alpha-Me-D-Asp-OH is suitable for chemical biology workflows that require incorporation of a stereodefined Asp-like motif into labeled peptides or biomolecule-modifying constructs. The β-carboxylate functionality can be converted into activated ester or amide-forming intermediates for conjugation handles, while the α-methyl-stabilized chiral center can help preserve defined stereochemistry during downstream coupling. N-protection and orthogonal carboxyl protection strategies support sequential installation of linkers, affinity tags, or reporter groups without scrambling stereochemical integrity. Labeled products derived from H-alpha-Me-D-Asp-OH can serve as tools for mapping binding interfaces, monitoring peptide uptake, or generating defined standards for biochemical assays.

4. Process Chemistry Intermediate

H-alpha-Me-D-Asp-OH is used as a chiral amino acid intermediate in process chemistry and fine chemical synthesis where stereochemical control and functional-group management are central to scalable manufacturing routes. The free carboxylic acid and amino functionality allow conversion into protected derivatives and activated intermediates that can be processed through multi-step sequences while maintaining D-configuration. The α-methyl substitution provides a robust handle for designing routes to sterically biased Asp analogs, which can be incorporated into larger peptide or peptidomimetic intermediates used in downstream production. The compound's functional-group pattern supports orthogonal protection planning for selective activation steps, aligning with industrial needs for reproducible intermediate handling and predictable chemoselectivity.

5. Analytical Standards

H-alpha-Me-D-Asp-OH is applied in analytical research as a stereochemically defined reference material for method development and characterization of Asp-containing peptides and derivatized analogs. The D-configuration and α-methyl substitution create a distinct mass and stereochemical signature that can improve identification and quantitation in chromatographic and spectrometric workflows. Carboxyl and amino functional groups enable conversion into derivatized standards that match the chemical forms encountered during peptide synthesis, including protected or activated forms used as coupling partners. Reference materials derived from H-alpha-Me-D-Asp-OH can support verification of stereochemical integrity, monitoring of side reactions, and calibration of analytical methods used to characterize peptide building blocks and intermediates.

1. Relatedness of antibodies to peptides containing homocitrulline or citrulline in patients with rheumatoid arthritis

2. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

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

4. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

5. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)