Name: China Factory Supply High Purity D-tert-Butylglycine CAS 26782-71-8
Brand: Wuhan Fortuna Chemical Co., Ltd.

D-tert-Butylglycine (D-tBuGly or D-Tle) is a synthetic, non-proteinogenic amino acid characterized by its specific structure and properties. Here's a breakdown:

Core Structure: It's an alpha-amino acid, meaning it has an amino group (-NH₂), a carboxylic acid group (-COOH), and a side chain attached to the central alpha-carbon.

Side Chain: Its defining feature is a bulky tert-butyl group (-C(CH₃)₃) attached directly to the alpha-carbon. This group is:

Highly hydrophobic: Repels water.
Sterically bulky: Takes up a lot of space.
Stereochemistry: The "D-" prefix specifies its stereochemistry. It is the dextrorotatory enantiomer, meaning it rotates plane-polarized light to the right. This is the mirror-image form not commonly found in natural proteins (which primarily use L-amino acids).

Chemical Structure:

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HO-C-C*-NH₂

(CH₃)₃C

Key Properties and Significance:

High Steric Hindrance: The large, branched tert-butyl group creates significant steric bulk around the alpha-carbon. This severely restricts the conformational flexibility (rotation around bonds) of any peptide chain it's incorporated into.

Hydrophobicity: The tert-butyl group is strongly hydrophobic, making D-tBuGly and peptides containing it less soluble in water.

Unnatural Configuration: The D-configuration makes it unrecognizable to most natural biological systems that process L-amino acids (like ribosomes and many proteases).

Primary Uses in Research & Chemistry:

Peptide Engineering & Conformational Control:

Inducing/Stabilizing Beta-Turns: Its bulk and restricted flexibility are often used to force or stabilize specific turns (especially Type II' beta-turns) in peptide backbones, crucial for mimicking bioactive peptide structures.
Creating Peptidomimetics: Used to design modified peptides (peptidomimetics) with enhanced stability, altered activity, or specific 3D shapes that natural amino acids can't achieve.
Reducing Conformational Flexibility: Limits the number of possible conformations a peptide can adopt, simplifying structural studies or locking peptides into a bioactive shape.
Enhancing Proteolytic Stability: The combination of D-configuration and bulky side chain makes peptides containing D-tBuGly highly resistant to degradation by most proteolytic enzymes (proteases), increasing their half-life in vivo.
Studying Enzyme Specificity & Protein Folding: Used as a probe to understand how enzymes recognize substrates or how proteins fold, due to its unnatural size and stereochemistry.
Modulating Peptide Properties: Its hydrophobicity can be exploited to influence peptide solubility, membrane permeability, and interactions with hydrophobic targets or environments.

Synthesis:
D-tert-Butylglycine is not found naturally and is synthesized chemically in the laboratory. Common methods include:

Strecker Synthesis: Using tert-butyl aldehyde (pivalaldehyde), ammonia, and cyanide.
Alkylation of Glycine Equivalents: Alkylating a glycine synthon (like a Schiff base or oxazinone) with tert-butyl halide.
Resolution: Synthesizing the racemic mixture (DL-tert-butylglycine) and then separating the D-enantiomer using chiral techniques.

In summary: D-tert-Butylglycine is a valuable synthetic tool in peptide chemistry and drug design. Its unique combination of a bulky, hydrophobic tert-butyl group and the unnatural D-configuration provides powerful ways to control peptide conformation, enhance stability against enzymatic breakdown, and create novel bioactive molecules with tailored properties.