N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine
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N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine

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

Category
CBZ-Amino Acids
Catalog number
BAT-006000
CAS number
144317-18-0
Molecular Formula
C32H30N2O5
Molecular Weight
522.59
N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine
IUPAC Name
(2S)-4-[[(4-methylphenyl)-diphenylmethyl]amino]-4-oxo-2-(phenylmethoxycarbonylamino)butanoic acid
Synonyms
Z-Asn(Mtt)-OH; Z-Asn(MeTrt)-OH
Purity
99%
Density
1.238±0.06 g/cm3
Boiling Point
783.9±60.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C32H30N2O5/c1-23-17-19-27(20-18-23)32(25-13-7-3-8-14-25,26-15-9-4-10-16-26)34-29(35)21-28(30(36)37)33-31(38)39-22-24-11-5-2-6-12-24/h2-20,28H,21-22H2,1H3,(H,33,38)(H,34,35)(H,36,37)/t28-/m0/s1
InChI Key
OOWKUTRZJDOGPF-NDEPHWFRSA-N
Canonical SMILES
CC1=CC=C(C=C1)C(C2=CC=CC=C2)(C3=CC=CC=C3)NC(=O)CC(C(=O)O)NC(=O)OCC4=CC=CC=C4

N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine, a chemical compound widely utilized in peptide synthesis and pharmaceutical research, possesses diverse applications. Here are the key applications expressed with heightened perplexity and burstiness:

Peptide Synthesis: Serving as a protected amino acid derivative in peptide synthesis, N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine plays a pivotal role. Its strategic protecting groups shield the amino and carboxyl ends during peptide chain elongation, ensuring the successful assembly of intricate peptides with exceptional yield and purity.

Drug Discovery: Within the realm of pharmaceutical research, N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine drives the development of peptide-centric drugs. By integrating it into peptide libraries, researchers embark on a quest to unearth bioactive sequences that may harbor therapeutic potential. This molecule’s integration into combinatorial chemistry expedites the discovery of novel lead compounds, hastening progress in drug innovation.

Proteomics: Critical for deciphering protein interactions and functions, N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine finds its niche. Its inclusion in synthetic peptides facilitates precise exploration of protein domains and the mapping of interaction sites. This capability aids in unraveling the intricate roles of specific proteins within complex biological systems, shedding light on the molecular intricacies of life.

Biomedical Engineering: Beyond peptides, this compound extends its influence to the realm of biomaterial design and synthesis. By incorporating N-α-Carbobenzoxy-N-β-(4-methyltrityl)-L-asparagine into peptide-based scaffolds, researchers craft materials boasting enhanced biological compatibility and functionality. These innovative biomaterials hold promise for applications in tissue engineering and regenerative medicine, heralding a new era of bioengineering advancements.

1. The kinetics of the removal of the N-methyltrityl (Mtt) group during the synthesis of branched peptides
D Li, D L Elbert J Pept Res. 2002 Nov;60(5):300-3. doi: 10.1034/j.1399-3011.2002.21018.x.
The purpose of this short communication is to describe the reaction rate for the removal of the N-methyltrityl (Mtt) protecting group that is used in solid-phase peptide synthesis for the production of branched and cyclic peptides. The reaction rate was observed to follow zero-order kinetics, and we suggest the optimal conditions for the removal of the Mtt group in batchwise synthesis.
2. Novel N omega-xanthenyl-protecting groups for asparagine and glutamine, and applications to N alpha-9-fluorenylmethyloxycarbonyl (Fmoc) solid-phase peptide synthesis
Y Han, N A Solé, J Tejbrant, G Barany Pept Res. 1996 Jul-Aug;9(4):166-73.
The N alpha-9-fluorenylmethyloxycarbonyl (Fmoc), N omega-9H-xanthen-9-yl (Xan), N omega-2-methoxy-9H-xanthen-9-yl (2-Moxan) or N omega-3-methoxy-9H-xanthen-9-yl (3-Moxan) derivatives of asparagine and glutamine were prepared conveniently by acid-catalyzed reactions of appropriate xanthydrols with Fmoc-Asn-OH and Fmoc-Gln-OH. The Xan and 2-Moxan protected derivatives have been used in Fmoc solid-phase syntheses of several challenging peptides: a modified Riniker's peptide to probe tryptophanalkylation side reactions, Briand's peptide to assess deblocking, at the N-terminus and Marshall's ACP (65-74) to test difficult couplings. Removal of the Asn and Gln side-chain protection occurred concomitantly with release of peptide from the support, under the conditions for acidolytic cleavage of the tris(alkoxy)benzylamide (PAL) anchoring linkage by use of trifluoroacetic acid/scavenger mixtures. For each of the model peptides, the products obtained by the new protection schemes were purer than those obtained with N omega-2,4,6-trimethoxybenzyl (Tmob) or N omega-triphenylmethyl (Trt) protection for Asn and Gln.
3. Incomplete TFA deprotection of N-terminal trityl-asparagine residue in fmoc solid-phase peptide chemistry
M Friede, S Denery, J Neimark, S Kieffer, H Gausepohl, J P Briand Pept Res. 1992 May-Jun;5(3):145-7.
We demonstrate that TFA deprotection of trityl-protected N-terminal asparagine is incomplete under normal conditions, resulting in low yields or impure products. This phenomenon does not occur if the asparagine is internal, nor for trityl-protected N-terminal glutamine. Studies on the deprotection of H Asn(Trt)OH show that the incomplete deprotection is due to the extremely slow removal of a trityl group close to an amino group. The use of the new methyl-trityl protecting group overcomes this problem resulting in rapid and complete deprotection.
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