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Application Area

Nα-(tert-Butyloxycarbonyl)-Nα-benzyl-D-alanine

* 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-001318

CAS number

120571-59-7

Molecular Formula

C15H21NO4

Molecular Weight

279.33

IUPAC Name

(2R)-2-[benzyl-[(2-methylpropan-2-yl)oxycarbonyl]amino]propanoic acid

Synonyms

N-Boc-N-Bzl-D-alanine

Appearance

White crystalline powder

Purity

≥ 99% (HPLC)

Melting Point

116-123°C

Storage

Store at 2-8 °C

InChI

InChI=1S/C15H21NO4/c1-11(13(17)18)16(14(19)20-15(2,3)4)10-12-8-6-5-7-9-12/h5-9,11H,10H2,1-4H3,(H,17,18)/t11-/m1/s1

InChI Key

MYGPVQDUOSMACR-LLVKDONJSA-N

Canonical SMILES

CC(C(=O)O)N(CC1=CC=CC=C1)C(=O)OC(C)(C)C

Nα-(tert-Butyloxycarbonyl)-Nα-benzyl-D-alanine, a versatile chemical compound, widely utilized in peptide synthesis and diverse biochemical applications possesses myriad functionalities. Here are the key applications presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a pivotal element in solid-phase peptide synthesis, Nα-(tert-Butyloxycarbonyl)-Nα-benzyl-D-alanine acts as a foundational unit. It plays a critical role in ensuring the precise arrangement of amino acid residues during the synthesis procedure. Subsequently, the tert-butyloxycarbonyl (Boc) group is selectively removed to yield the final peptide construct marking the completion of the synthesis journey.

Pharmaceutical Research: Within the realm of drug discovery and development, this compound emerges as an indispensable player in the crafting of peptide-based pharmaceuticals. By manipulating the peptide structure, researchers can enhance attributes such as stability, efficacy and selectivity. Nα-(tert-Butyloxycarbonyl)-Nα-benzyl-D-alanine facilitates the integration of tailored modifications potentially leading to the creation of potent therapeutic agents with enhanced pharmacological profiles.

Bioconjugation: In the intricate domain of bioconjugation methodologies, Nα-(tert-Butyloxycarbonyl)-Nα-benzyl-D-alanine finds its utility in linking peptides to diverse molecules like drugs, fluorescent markers or targeting ligands. This linkage enables the formation of multifaceted biomolecules with applications spanning diagnostics, imaging and targeted therapy. The Boc group delivers temporary shelter to the amino group throughout the conjugation process ensuring precise and controlled bioconjugation outcomes.

Enzyme Studies: Expanding its reach into enzymology, Nα-(tert-Butyloxycarbonyl)-Nα-benzyl-D-alanine emerges as a fundamental tool for investigating enzyme-substrate interactions. Serving as an analog or inhibitor in enzymatic assays, it facilitates the evaluation of proteases and other enzyme activities with high specificity and precision. These investigations unravel essential insights into enzyme mechanisms ultimately contributing to the development of enzyme inhibitors tailored for therapeutic interventions.

1. p-Nitrobenzyl protection for cysteine and selenocysteine: a more stable alternative to the acetamidomethyl group

Markus Muttenthaler, Yesica Garcia Ramos, Debby Feytens, Aline D de Araujo, Paul F Alewood Biopolymers. 2010;94(4):423-32. doi: 10.1002/bip.21502.

This study evaluated the acidic lability of the acetamidomethyl (Acm), trimethylacetamidomethyl (Tacm), and the p-nitrobenzyl (pNB) as protecting groups for cysteine and selenocysteine (Sec) during the tert-butyloxycarbonyl (Boc)-chemistry solid-phase peptide synthesis of oxytocin (OT). Two novel Sec building blocks (Nalpha-tert-butyloxycarbonyl-Se(acetamidomethyl)-L-selenocysteine (Boc-L-Sec(Acm)-OH) and Nalpha-tert-butyloxycarbonyl-S(4-nitrobenzyl)-L-selenocysteine (Boc-L-Sec(pNB)-OH)) were developed for this study. Six partially protected thio- and seleno-OT analogues were synthesized, purified, and exposed to neat trifluoroacetic acid (TFA) at temperatures of 25, 40, 50, and 60 degrees C for 1 h, and HF treatment at 0 degrees C for 1 h. Significant losses were observed for the Acm and Tacm group in TFA at temperatures greater than 25 degrees C and during HF treatment at 0 degrees C, whereas the pNB group remained intact. Removal of the pNB was achieved via reduction to the p-aminobenzyl group either with zinc in acetic acid in solution or via tin chloride in hydrochloric acid on solid support, followed by oxidative cleavage with iodine yielding the corresponding disulfide or diselenide bond. No major side reactions were observed. This study confirms the occasionally described Acm instability and underpins the development of the pNB group as an alternative for cysteine and Sec protection.

3. Betidamino acids: versatile and constrained scaffolds for drug discovery

J E Rivier, G Jiang, S C Koerber, J Porter, L Simon, A G Craig, C A Hoeger Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2031-6. doi: 10.1073/pnas.93.5.2031.

Betidamino acids (a contraction of "beta" position and "amide") are N'-monoacylated (optionally, N'-monoacylated and N-mono- or N,N'-dialkylated) aminoglycine derivatives in which each N'acyl/alkyl group may mimic naturally occurring amino acid side chains or introduce novel functionalities. Betidamino acids are most conveniently generated on solid supports used for the synthesis of peptides by selective acylation of one of the two amino functions of orthogonally protected aminoglycine(s) to generate the side chain either prior to or after the elongation of the main chain. We have used unresolved Nalpha-tert-butyloxycarbonyl-N'alpha-fluorenylmethoxycarbonyl++ + aminoglycine, and Nalpha-(Nalpha-methyl)-tert-butyloxycarbonyl-N'alpha-fluo renylmethoxycarbonyl aminoglycine as the templates for the introduction of betidamino acids in Acyline [Ac-D2Nal-D4Cpa-D3Pal-Ser-4Aph(Ac)-D4Aph(A c)-Leu-Ilys-Pro-DAla-NH2, where 2Nal is 2-naphthylalanine, 4Cpa is 4-chlorophenylalanine, 3Pal is 3-pyridylalanine, Aph is 4-aminophenylalanine, and Ilys is Nepsilon-isopropyllysine], a potent gonadotropin-releasing hormone antagonist, in order to test biocompatibility of these derivatives. Diasteremneric peptides could be separated in most cases by reverse-phase HPLC. Biological results indicated small differences in relative potencies (<5-fold) between the D and L nonalkylated betidamino acid-containing Acyline derivatives. Importantly, most betide diastereomers were equipotent with Acyline. In an attempt to correlate structure and observed potency, Ramachandran-type plots were calculated for a series of betidamino acids and their methylated homologs. According to these calculations, betidamino acids have access to a more limited and distinct number of conformational states (including those associated with alpha-helices, beta-sheets, or turn structures), with deeper minima than those observed for natural amino acids.