Boc-Aib-OH CAS 30992-29-1

Boc-Aib-OH acts as a protected amino acid that can be effectively utilized in the synthesis of peptides and proteins. The Boc (tert-butyloxycarbonyl) group specifically protects the amino functionality of the molecule, thereby allowing chemists to selectively manipulate other functional groups during the peptide synthesis process without unwanted side reactions.

Once the desired peptide sequence is fully constructed, the Boc protecting group can be easily removed using mild acidic conditions (such as trifluoroacetic acid), which releases the free amino acid. This free amino group then enables further modifications or direct use in various biological applications.

Derivatives of Boc-Aib-OH have gained significant traction in drug discovery and pharmaceutical chemistry, largely due to their unique chemical structure and versatile biological properties. Aib itself is a non-natural amino acid characterized by two methyl groups attached to the -carbon, which confers increased conformational rigidity to peptide chains when incorporated-this rigidity can enhance the peptide's resistance to enzymatic degradation (e.g., by proteases) and improve its binding affinity to target biomolecules, such as receptors or enzymes.

As a versatile building block, Boc-Aib-OH and its derivatives are widely used in the synthesis of complex organic molecules with potential therapeutic effects.

For instance, they are frequently employed in the development of peptide-based drugs, including antimicrobial peptides, hormone analogs, and anti-cancer peptides, where the Aib residue's non-natural side chain can impart novel biological activities that natural amino acids cannot achieve. The Boc protecting group is particularly valuable in this context, as it allows for the controlled incorporation of Aib into the peptide drug or drug candidate during synthesis, ensuring the correct sequence and structure are maintained. Additionally, the ability to easily remove the Boc group post-synthesis enables further optimization of the drug molecule, such as the introduction of pharmacophores or modifications to improve solubility and pharmacokinetic properties.

Beyond its applications in biochemistry and drug development, Boc-Aib-OH also serves as a functional monomer in the synthesis of polymers and copolymers, contributing to the development of advanced materials with tailored properties. Its unique chemical structure-combining the protected amino group and the rigid Aib backbone-makes it an ideal candidate for incorporating into polymer chains, as it can modulate the physical, chemical, and mechanical properties of the resulting materials.

When incorporated into polymer chains, the Aib moiety can enhance the polymer's thermal stability, rigidity, and resistance to chemical degradation, while the Boc group can act as a reactive site for further functionalization.

These modified polymers find diverse applications across various fields: in biomaterials, for example, they are used in the development of biocompatible scaffolds for tissue engineering, drug delivery systems, or medical devices, where their non-toxic nature and structural stability are critical. In addition, they are employed in the production of specialized coatings and adhesives, where their unique surface properties (e.g., hydrophobicity, adhesion strength) make them suitable for industrial or consumer applications, such as corrosion-resistant coatings or high-performance adhesives for advanced materials.

Boc-Aib-OH is also widely recognized as a valuable research tool in various biochemical, chemical, and biophysical studies, owing to its distinct chemical structure and predictable reactivity. Its non-natural Aib residue, with its , -disubstituted structure, makes it a useful probe for investigating the structure-function relationships of peptides and proteins-for example, researchers can use Boc-Aib-OH to introduce conformational constraints into peptide chains, allowing them to study how structural rigidity affects a peptide's biological activity or interaction with target molecules.

Furthermore, its Boc-protected amino group provides a reliable model for studying protecting group chemistry, including the development of new deprotection methods or the optimization of existing ones. In mechanistic studies, Boc-Aib-OH is often used to elucidate the pathways of peptide bond formation, deprotection reactions, and other key processes in organic and peptide chemistry. It also serves as a standard reagent in reaction optimization, where its well-characterized reactivity allows chemists to test and refine reaction conditions (e.g., temperature, solvent, catalyst) for more efficient synthesis of peptides, polymers, or other organic compounds. Overall, its versatility and predictability make it an indispensable tool for advancing research in multiple scientific disciplines.

The oral administration of LD ₅₀ to rats is not clear, but at a dose of 500 mg/kg, reduced activity, rapid breathing, tremors, and some animals died. Dissection revealed vacuolization of liver cells and edema of renal tubular epithelial cells.
Dogs are more sensitive to Boc Ab OH, with vomiting and diarrhea occurring after continuous administration of 100 mg/kg/d for 7 days, which may be related to differences in metabolic enzymes between species.

Administration of 100 mg/kg/d to rats for 13 weeks resulted in a decrease in testicular weight and sperm count in males, while no abnormalities were observed in the female ovaries. However, the incidence of estrous cycle disorders increased by 20%.
Neurobehavioral tests showed that the animals in the treatment group had a 30% reduction in activity distance during the open field experiment, indicating anxiety like behavior.

After exposure to 50 μ M Boc Ab OH for 24 hours, HepG2 cells showed a 50% decrease in cell viability, accompanied by a 2.5-fold increase in ROS generation and 60% depletion of GSH.
Co culture experiments have shown that pro-inflammatory cytokines (such as IL-6 and TNF - ) released by damaged liver cells can induce apoptosis of adjacent normal cells, forming "paracrine toxicity".