DL-2-Methylserine

DL-2-Methylserine is a serine-derived amino acid analog bearing a chiral 2-methyl substituent on the α-carbon and a side-chain hydroxymethyl group, giving it the general amino acid functionality of an amino group and a carboxylic acid (or corresponding ester/amide forms depending on derivatization). The presence of the additional methyl substituent increases steric demand around the stereocenter and can influence conformational preferences relative to serine, while the hydroxyl-bearing side chain enables hydrogen-bonding and straightforward functional group transformations. As a DL mixture, the compound contains both enantiomers, which is relevant for studies requiring racemic incorporation or for downstream resolution strategies to access stereodefined 2-methylserine building blocks. The amino acid framework supports standard peptide-coupling chemistries after appropriate protection of the amine and carboxyl functionality, making it a practical intermediate for amino acid derivatization and peptide science.

1. Peptide Synthesis

DL-2-Methylserine is applied in peptide building block preparation where α-amino acid coupling to form amide bonds is required, and its serine-like side-chain hydroxyl can be selectively protected to control chemoselectivity during stepwise synthesis. The amino and carboxyl functionalities allow conversion into N-protected amino acid derivatives and C-terminal activated forms, supporting peptide coupling strategies compatible with common peptide coupling reagents. The added 2-methyl stereocenter can be incorporated into peptide backbones to probe steric effects on conformation and intramolecular hydrogen bonding patterns involving the side-chain hydroxyl. Downstream, protected DL-2-methylserine residues can be used to generate peptide analogs for biochemical research and SAR studies where racemic incorporation is acceptable or where later enantiomer separation is planned.

2. Side-Chain Functionalization

DL-2-Methylserine is used for amino acid derivatization workflows targeting side-chain hydroxyl chemistry, including etherification, ester formation, and conversion to leaving groups for further substitution. The hydroxymethyl group can be protected and deprotected to enable controlled introduction of polar or hydrophobic substituents, while maintaining the amino acid core for subsequent coupling or analytical derivatization. The α-methyl substituent can modulate reactivity by affecting local sterics around the functionalized side chain, which can be relevant when designing fragments for peptidomimetic construction. Resulting derivatives serve as intermediates for generating functional amino acid analogs, solubility-tuned peptide fragments, and chemically defined standards for monitoring hydroxyl-based transformations in synthetic organic chemistry.

3. Chiral Building Block Development

DL-2-Methylserine is suitable for chiral synthesis and stereochemical studies because the racemic mixture can be resolved or converted into diastereomeric derivatives for enantiomer discrimination. The single stereocenter at C-2 provides a clear handle for downstream stereochemical control, enabling preparation of stereodefined 2-methylserine derivatives used in enantioselective peptide construction and stereochemical SAR investigations. N- and O-protection strategies can be employed to stabilize the amino acid during resolution, activation, and peptide coupling, while minimizing epimerization risk under appropriate conditions. Enantiopure downstream products can then be incorporated into peptides and peptidomimetics to support structure-function mapping where stereochemistry at the α-carbon is a key design variable.

4. Chemical Biology Research

DL-2-Methylserine is applied in chemical biology research as a serine analog for introducing hydroxyl-bearing residues with altered steric profile into peptide scaffolds and protein-interaction probes. The amino acid backbone supports incorporation into modified peptides that can participate in hydrogen-bonding networks and side-chain recognition motifs, while the 2-methyl substitution can shift local geometry and affect binding conformations. The side-chain hydroxyl enables attachment of tags or reactive handles after controlled protection, supporting downstream conjugation to affinity probes or labeling reagents. Generated peptide-based tools can be used to interrogate substrate tolerance, binding preferences, and recognition patterns in biochemical assays where an amino acid analog with a hydroxymethyl group is required.

5. Pharmaceutical Intermediate Preparation

DL-2-Methylserine is relevant to pharmaceutical intermediate preparation and process chemistry as a chiral amino acid precursor platform that can be transformed into protected amino acid derivatives for controlled manufacturing routes. The amino acid's functional groups support conversion into N-protected intermediates and activated carboxyl derivatives, enabling incorporation into larger fragments used in peptidic or peptidomimetic synthesis. The hydroxyl-bearing side chain can be managed through protection-group selection to ensure compatibility with multi-step coupling and deprotection sequences, while the α-methyl stereocenter provides a structural motif that can be retained or resolved depending on target specifications. Downstream, stereodefined or racemic 2-methylserine-containing intermediates can be used to build well-defined molecular entities for fine chemical synthesis and applied product development workflows.

1. Olfactory receptor based piezoelectric biosensors for detection of alcohols related to food safety applications

2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function

3. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die

4. TMEM16F and dynamins control expansive plasma membrane reservoirs

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