D-Homoserine TCI H1224

D-Homoserine is a non-proteinogenic amino acid in the D configuration whose structure resembles serine, but with a hydroxyalkyl side chain one carbon atom longer. This small difference carries significant consequences in peptide chemistry, because a hydroxyl group positioned further from the backbone alters geometry, hydrogen-bonding capability, and the tendency toward cyclization into a lactone. In the laboratory, this compound is used as a building block for assembling modified peptides and for studying the role of stereochemistry in molecular recognition.

The main reason for choosing the D form is its resistance to proteases, which naturally recognize only L-amino acids. Peptides containing D residues generally have a longer lifetime in biological systems and can adopt conformations that are not accessible to purely L-configured sequences. Homoserine itself is an important intermediate in the biosynthesis of the aspartate family of amino acids, so its D enantiomer is useful as a comparator in enzymology studies and stereochemical selectivity assays. As a solid, the compound is easy to weigh, easy to store, and compatible with solid-phase peptide synthesis protocols.

In Indonesian laboratories, this material is typically found in university peptide chemistry groups, biochemistry and enzymology research units, and institutional laboratories working on protein and amino acid studies. It is generally ordered in research quantities for method development, comparative stereochemistry work, and the preparation of modified peptide sequences. Handling in these settings follows standard reagent-grade practice, with the solid weighed out as needed and the remainder returned to controlled storage.

• Solid-phase peptide synthesis: serves as a D-configured building block for assembling modified peptide sequences that require a longer hydroxyalkyl side chain than serine provides.
• Protease resistance studies: the D configuration is not recognized by proteases that act only on L-amino acids, allowing researchers to prepare peptides with extended lifetimes in biological systems.
• Conformational research: D residues permit peptides to adopt backbone geometries that purely L-configured sequences cannot reach, making this compound useful for structural investigations.
• Enzymology comparator work: as the D enantiomer of an intermediate in aspartate-family amino acid biosynthesis, it serves as a reference compound in enzyme mechanism and activity studies.
• Stereochemical selectivity assays: the compound acts as a defined counter-enantiomer for testing how strongly a binding site or catalyst discriminates between D and L amino acid substrates.

Store the container tightly closed in a cool, dry place away from moisture, following the conditions given on the manufacturer's label. As a solid amino acid, the material is straightforward to weigh, but the container should be kept sealed between uses to limit moisture uptake. Use clean, dry spatulas and glass or chemically compatible plastic containers when transferring portions, and avoid returning removed material to the original container. Weighing is best carried out in a well-ventilated area or a fume hood to avoid inhaling fine dust. Wear a laboratory coat, safety glasses, and suitable gloves throughout handling, and consult the manufacturer's safety data sheet before first use.

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