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Boc-Ala[3-(1-THQ)]-OH

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

BOC-Amino Acids

Catalog number

BAT-000929

Molecular Formula

C17H24N2O4

Molecular Weight

320.38

Synonyms

Boc-Ala[3-(1,2,3,4-tetrahydroquinolin-1-yl)]-OH; N-α-(t-Butoxycarbonyl)-3-(1,2,3,4-tetrahydroquinolin-1-yl)-L-alanine; (2S)-3-(3,4-Dihydro-2H-quinolin-1-yl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid

Storage

Store at 2-8 °C

Boc-Ala[3-(1-THQ)]-OH, a derivative of modified amino acid, plays a crucial role in peptide synthesis and chemical research. Here are its versatile applications presented with high perplexity and burstiness:

Peptide Synthesis: At the forefront of peptide synthesis, Boc-Ala[3-(1-THQ)]-OH serves as a fundamental building block in creating peptides and small proteins. Its unique molecular structure enables the incorporation of non-standard amino acids into peptide sequences, broadening the diversity and functionality of synthesized peptides. Researchers harness this modified amino acid to engineer peptides with heightened biological activity or stability, pushing the boundaries of peptide design and function.

Drug Development: In the realm of pharmaceutical innovation, Boc-Ala[3-(1-THQ)]-OH is a key player in crafting novel therapeutic peptides. These peptides target specific receptors or enzymes, laying the groundwork for pioneering treatments for diseases like cancer and infectious diseases. The modified amino acid holds promise for enhancing the efficacy and specificity of peptide-based drugs, driving forward the development of precision medicine and personalized therapies.

Structural Biology: Delving into the intricate world of protein structure and dynamics, Boc-Ala[3-(1-THQ)]-OH is a vital tool for researchers. By integrating this modified amino acid into proteins, scientists can delve into protein folding conformational changes and interactions with other molecules. This knowledge is essential for unraveling the fundamental principles of protein behavior and designing molecules that can modulate protein function, providing insights into the inner workings of biological systems.

Bioconjugation: A pivotal component in bioconjugation techniques, Boc-Ala[3-(1-THQ)]-OH drives the attachment of peptides or proteins to diverse molecules, such as drugs nanoparticles or imaging agents. This process gives rise to multifunctional biomolecules with enhanced targeting capabilities and therapeutic potential. Serving as a versatile linker, the modified amino acid facilitates the development of cutting-edge biotechnological applications, paving the way for innovative advancements in targeted drug delivery and therapeutic interventions.

1. [Peptide derivatives of tylosin-related macrolides]

G A Korshunova, N V Sumbatian, N V Fedorova, I V Kuznetsova, A V Shishkina, A A Bogdanov Bioorg Khim. 2007 Mar-Apr;33(2):235-44. doi: 10.1134/s1068162007020033.

Approaches to the synthesis of model compounds based on the tylosin-related macrolides desmycosin and O-mycaminosyltylonolide were developed using specially designed peptide derivatives of macrolide antibiotics to study the conformation and topography of the nascent peptide chain in the ribosome tunnel. A method for selective bromoacetylation of desmycosin at the hydroxyl group of mycinose was developed, which involves preliminary acetylation of mycaminose. The reaction of the 4"-bromoacetyl derivative of the antibiotic with cesium salts of the dipeptide Boc-Ala-Ala-OH and the hexapeptide MeOTr-Gly-Pro-Gly-Pro-Gly-Pro-OH led to the corresponding peptide derivatives of desmycosin. The protected peptides Boc-Ala-Ala-OH, Boc-Ala-Ala-Phe-OH, and Boc-Gly-Pro-Gly-Pro-Gly-Pro-OH were condensed with the C23-hydroxyl group of O-mycaminosyltylonolide.

2. Hybrid peptide design. Hydrogen bonded conformations in peptides containing the stereochemically constrained gamma-amino acid residue, gabapentin

Prema G Vasudev, Kuppanna Ananda, Sunanda Chatterjee, Subrayashastry Aravinda, Narayanaswamy Shamala, Padmanabhan Balaram J Am Chem Soc. 2007 Apr 4;129(13):4039-48. doi: 10.1021/ja068910p. Epub 2007 Mar 10.

The crystal structure of 12 peptides containing the conformationally constrained 1-(aminomethyl)cyclohexaneacetic acid, gabapentin (Gpn), are reported. In all the 39 Gpn residues conformationally characterized so far, the torsion angles about the Calpha-Cbeta and Cbeta-Cgamma bonds are restricted to the gauche conformation (+/-60 degrees ). The Gpn residue is constrained to adopt folded conformations resulting in the formation of intramolecularly hydrogen-bonded structures even in short peptides. The peptides Boc-Ac6c-Gpn-OMe 1 and Boc-Gpn-Aib-Gpn-Aib-OMe 2 provide examples of C7 conformation; peptides Boc-Gpn-Aib-OH 3, Boc-Ac6c-Gpn-OH 4, Boc-Val-Pro-Gpn-OH 5, Piv-Pro-Gpn-Val-OMe 6, and Boc-Gpn-Gpn-Leu-OMe 7 provide examples of C9 conformation; peptide Boc-Ala-Aib-Gpn-Aib-Ala-OMe 8 provides an example of C12 conformation and peptides Boc-betaLeu-Gpn-Val-OMe 9 and Boc-betaPhe-Gpn-Phe-OMe 10 provide examples of C13 conformation. Gpn peptides provide examples of backbone expanded mimetics for canonical alpha-peptide turns like the gamma (C7) and the beta (C10) turns. The hybrid betagamma sequences provide an example of a mimetic of the C13 alpha-turn formed by three contiguous alpha-amino acid residues. Two examples of folded tripeptide structures, Boc-Gpn-betaPhe-Leu-OMe 11 and Boc-Aib-Gpn-betaPhg-NHMe 12, lacking internal hydrogen bonds are also presented. An analysis of available Gpn residue conformations provides the basis for future design of folded hybrid peptides.

3. Correlations between steric/thermochemical parameters and O-/N-acylation reactions of cellulose

Kesavan Devarayan, Taketoshi Hayashi, Masakazu Hachisu, Jun Araki, Kousaku Ohkawa Carbohydr Polym. 2013 Apr 15;94(1):468-78. doi: 10.1016/j.carbpol.2012.12.074. Epub 2013 Jan 16.

N(α)-t-Butyloxycarbonyl (Boc)-amino acids (Xaa = Gly, Ala, or β-Ala) were reacted with the cellulose hydroxyl groups (O-acylation) using N,N'-carbonyl diimidazole. The degrees of substitution toward the total hydroxyl groups (DS%(/OH)s) were 38% for O-(Boc-Gly)-Cellulose, 29% for O-(Boc-Ala)-Cellulose and 53% for O-(Boc-β-Ala)-Cellulose. The one-by-one N-acylation between the O-(Xaa)-Celluloses and Boc-Ala-Gly using a water-soluble carbodiimide yielded the conjugates N-(Boc-Ala-Gly)-Xaa-Celluloses with DS%(/NH2) values of 25% (Xaa = Gly), 35% (Ala), and 48% (β-Ala), respectively. The results were well correlated with ΔG and ΔEstrain profiles, which were predicted by semi-empirical thermochemical parameter calculation coupled with conformer search (R(2)>0.90). N-acylation of the O-(β-Ala)-Cellulose using various length of oligo-peptides, Boc-(Ala-Gly)n and Boc-(Gly-Ala)n (where, n = 0.5, 1.0, 1.5, 2.0, 3.0), suggested that the DS%(/NH2) was dependent on the structural features of the symmetric anhydrides as the N-acylating agents, including conformer populations and their transition energy.