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Application Area

Nα-Trityl-L-asparagine

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

Category

β−Amino Acids

Catalog number

BAT-007743

CAS number

132388-58-0

Molecular Formula

C23H22N2O3

Molecular Weight

374.43

IUPAC Name

(2S)-2-amino-4-oxo-4-(tritylamino)butanoic acid

Synonyms

Trt-L-Asn-OH; Trt-(S)-2-aminosuccinic acid 4-amide; H-Asn(Trt)-OH; N'-Trityl-L-asparagine; J-300055; Trt L Asn OH; (2S)-2-amino-3-[(triphenylmethyl)carbamoyl]propanoic acid; H-Asn(Trt)-2-Chlorotrityl Resin; N-beta-Trityl-L-asparagine; h-asn(trt)oh; (2S)-2-amino-4-oxo-4-(tritylamino)butanoic acid

Appearance

White crystalline powder

Purity

≥ 95%

Density

1.234±0.06 g/cm3 (Predicted)

Melting Point

155-162 °C

Boiling Point

641.2±55.0 °C (Predicted)

Storage

Store at 2-8 °C

InChI

InChI=1S/C23H22N2O3/c24-20(22(27)28)16-21(26)25-23(17-10-4-1-5-11-17,18-12-6-2-7-13-18)19-14-8-3-9-15-19/h1-15,20H,16,24H2,(H,25,26)(H,27,28)/t20-/m0/s1

InChI Key

BRRPJQYCERAMFI-FQEVSTJZSA-N

Canonical SMILES

C1=CC=C(C=C1)C(C2=CC=CC=C2)(C3=CC=CC=C3)NC(=O)CC(C(=O)O)N

Nα-Trityl-L-asparagine, a protected amino acid derivative crucial in peptide synthesis and other biochemical endeavors, finds diverse applications. Here are four key applications presented with high perplexity and burstiness:

Peptide Synthesis: Embedded within solid-phase peptide synthesis, Nα-Trityl-L-asparagine plays a pivotal role in introducing asparagine residues into peptide chains. The trityl group acts as a shield, safeguarding the amino group from unwanted reactions throughout the synthesis journey. Upon completion, this protective layer can be selectively removed, unveiling the meticulously crafted peptide, ready to unveil its structural intricacies.

Protein Engineering: In the realm of protein engineering, Nα-Trityl-L-asparagine emerges as a versatile tool for manipulating and fabricating proteins with tailored sequences. This capability empowers researchers to embed asparagine at specific sites within proteins, facilitating detailed investigations into protein folding, stability, and functionality. Such strategic alterations hold the key to crafting proteins endowed with enhanced therapeutic or industrial attributes, propelling innovation in diverse sectors.

Combinatorial Chemistry: A cornerstone of combinatorial chemistry, Nα-Trityl-L-asparagine contributes significantly to the creation of expansive peptide libraries brimming with structural diversity. Through systematic integration into various peptide sequences, this protected amino acid serves as a catalyst for exploring intricate structure-activity relationships. This methodology is instrumental in pinpointing potential peptide candidates with noteworthy biological activities or therapeutic potentials, fueling advancements in drug discovery and development.

Bioconjugation: Embraced within bioconjugation methodologies, Nα-Trityl-L-asparagine facilitates the coupling of peptides to a myriad of biomolecules or surfaces with precision and efficiency. The trityl-protected asparagine orchestrates specific and effective conjugation reactions, ensuring targeted outcomes. This application stands at the forefront of crafting bespoke drug delivery systems, diagnostic tools, and biosensors, driving forward the frontiers of biomedical applications.

1.Incomplete trifluoroacetic acid deprotection of asparagine-trityl-protecting group in the vicinity of a reduced peptide bond.

Quesnel A1, Briand JP. J Pept Res. 1998 Aug;52(2):107-11.

During the Fmoc solid-phase synthesis of reduced peptide bond analogues, we observed that the trityl protection of an asparagine residue in the vicinity of a reduced peptide bond is not cleaved completely after the final trifluoroacetic acid deprotection step. The relative position of the Asn side-chain amine and of the aminomethylene bond as well as the preferential protonation of the secondary amine can be used to explain this phenomenon. We show that longer deprotection times or the use of methyl-trityl protection partially improves the yield of the Asn-deprotected peptide whereas xanthenyl protection totally overcomes this problem.

2.Aminonitriles and aminothioamides related to natural amino acids.

Banerjee SN, Ressler C. Int J Pept Protein Res. 1979;14(3):234-46.

N-p-Methoxybenzyloxycarbonyl and N-tert.-butyloxycarbonyl amino acid amides related to a series of natural amino acids were dehydrated to the corresponding Meoz- and Boc-alpha-aminonitriles. Deprotection of the latter derivatives afforded alpha-aminonitriles related to alanine, tyrosine, phenylalanine, dihydrophenylalanine, histidine, Dopa, ornithine, asparagine and glutamine. Thioamidation with H2S/NH3 or H2S/NEt3 in general converted the protected amino nitriles to Meoz- and Boc-alpha-aminothioamides. When deprotected these furnished the alpha-aminothioamides corresponding to alanine, tyrosine, phenylalanine, dihydrophenylalanine and histidine. For dehydration and thioamidation of histidine and Dopa, N alpha-Boc-im trityl-histidine and N-Boc-O, O'-diacetyldihydroxyphenylalanine were useful. Dopa was obtained as the free and Boc-thiohydrazide. Also prepared were N alpha,omega-diMeoz-ornithine DCHA, Meoz-2,5-dihydrophenylalanine DCHA and N,O-diMeoz-tyrosine as starting materials and N,O-dicarbobenzyloxycarbonyltyrosinamide, N,O-diZ-tyrosine nitrile and Z-beta-cyano-beta-alaninamide as model compounds.

3.Protection of asparagine and glutamine during N alpha-Bpoc-based solid-phase peptide synthesis.

Carey RI, Huang H, Wadsworth JL, Burrell CS. Int J Pept Protein Res. 1996 Mar;47(3):209-13.

In this paper we describe the synthesis and properties of Bpoc-Asn(Trt)-OH, Bpoc-Asn(Trt)-OPfp, Bpoc-Gln(Trt)-OH and Bpoc-Gln(Trt)-OPfp. These derivatives are highly soluble in CH2Cl2 and can be coupled efficiently in solid-phase peptide synthesis. The peptides, acetyl-Ala-Phe-Asn(Trt)-Gly-Leu-Ala-O-Dbf-SH and Boc-Cys(Acm)-Ala-Phe-Gln(Trt)-Gly-Leu-Ala-O-Dbf-SH (where O-Dbf-SH is the peptide ester of 4-mercapto-6-hydroxydibenzofuran) were synthesized by stepwise solid-phase peptide synthesis using N alpha-Bpoc amino acids. We have observed that less than 0.1% of the trityl group is removed from the carboxamide of Gln and Asn during a standard 15 min N alpha-Bpoc deprotection in 0.5% TFA in CH2Cl2.

4.4-Methyltrityl (Mtt): a new protecting group for the side chain protection of Asn and Gln in solid-phase peptide synthesis.

Sax B1, Dick F, Tanner R, Gosteli J. Pept Res. 1992 Jul-Aug;5(4):245-6.

The trityl group was recently introduced for the protection of the side chain carboxamide function of asparagine and glutamine. The 4-methyltrityl (Mtt) group, a structural modification of trityl, is presented here and allows more rapid cleavage from the protected peptides. Procedures for the introduction of the group and comparative cleavage reactions are also presented.