102747-84-2

Usage

Uses

Used in Pharmaceutical Industry:
H-Gln(Trt)-OH is used as a building block for the production of peptides and proteins, playing a crucial role in the development of peptide-based drugs and pharmaceuticals. The trityl group's protective function ensures the successful synthesis of complex peptide structures, which are vital for various therapeutic applications.
Used in Peptide Synthesis:
H-Gln(Trt)-OH is utilized as a key reagent in solid-phase peptide synthesis, a technique that allows for the stepwise assembly of peptide chains. Its protective trityl group ensures that the amino group remains intact and unreacted until the desired point in the synthesis process, contributing to the successful construction of the peptide sequence.

InChI:InChI=1/C24H24N2O3/c25-21(23(28)29)16-17-22(27)26-24(18-10-4-1-5-11-18,19-12-6-2-7-13-19)20-14-8-3-9-15-20/h1-15,21H,16-17,25H2,(H,26,27)(H,28,29)/t21-/m0/s1

Upstream product

• 76-84-6 triphenylmethyl alcohol 
• 56-85-9 L-glutamine 
• 132327-80-1 Fmoc-L-Gln(Trt)-OH 
• 2650-64-8 Cbz-L-Gln 
• 132388-60-4 (S)-2-(((benzyloxy)carbonyl)amino)-5-oxo-5-(tritylamino)pentanoic acid 

Downstream Products

• 1403762-89-9 (S)-2-((1-((4-fluorobenzyl)carbamoyl)cyclopentyl)amino)-N₁-(furan-2-ylmethyl)-N₅-tritylpentanediamide 
• 1472653-60-3 (S)-2-azido-5-oxo-5-(tritylamino)pentanoic acid 
• 137348-91-5 Z-Pro-Gln(Trt)-OH 
• 132388-69-3 Boc-L-Gln(Trt)-OH 
• 1638884-71-5 N_α-(phenoxycarbonyl)-N_δ-trityl-L-glutamine 
• 1438859-93-8 (S)-2-hydroxy-5-oxo-5-(tritylamino)pentanoic acid 

Relevant academic research and scientific papers

Probing the role of backbone hydrogen bonds in protein-peptide interactions by amide-to-ester mutations

One of the most frequent protein-protein interaction modules in mammalian cells is the postsynaptic density 95/discs large/zonula occludens 1 (PDZ) domain, involved in scaffolding and signaling and emerging as an important drug target for several diseases

Learning from Peptides to Access Functional Precision Polymer Sequences

Functional precision polymers based on monodisperse oligo(N-substituted acrylamide)s and oligo(2-substituted-α-hydroxy acid)s have been synthesized. The discrete sequences originate from a direct translation of side-chain functionality sequences of a peptide with well-studied properties. The peptide was previously selected to solubilize the photosensitizer meta-tetra(hydroxyphenyl)chlorin. The resulting peptidomimetic formulation additives preserve the drug solubilization and release characteristics of the parent peptide. In some cases, superior properties are obtained, reaching up to 40 % higher payloads and 27-times faster initial drug release.

Mild oxidative cleavage of 9-BBN-protected amino acid derivatives

Protection of the amino acid moiety using 9-BBN is an effective method to enable side chain manipulations in synthesis of complex amino acids. We investigated the standard, mild method for deprotection of the 9-BBN group in methanolic chloroform, and found that it relies on a slow oxidation mediated by molecular oxygen. Building on this insight, we have developed a method that allows for a fast and selective deprotection using simple peroxy acid reagents. After Fmoc protection, products were isolated in >90% yield for a series of amino acid derivatives, including a galactosylated derivative of hydroxylysine. A representative set of 9-BBN-protected amino acid derivatives were efficiently deprotected using peracid reagents in excellent yields. Deprotection is orthogonal with several common protecting groups. Its tolerance of highly acid sensitive groups, such as trityl-protected amides and glycosidic linkages, is especially notable.

A mild removal of Fmoc group using sodium azide

A mild method for effectively removing the fluorenylmethoxycarbonyl (Fmoc) group using sodium azide was developed. Without base, sodium azide completely deprotected Nα-Fmoc-amino acids in hours. The solvent-dependent conditions were carefully studied and then optimized by screening different sodium azide amounts and reaction temperatures. A variety of Fmoc-protected amino acids containing residues masked with different protecting groups were efficiently and selectively deprotected by the optimized reaction. Finally, a biologically significant hexapeptide, angiotensin IV, was successfully synthesized by solid phase peptide synthesis using the developed sodium azide method for all Fmoc removals. The base-free condition provides a complement method for Fmoc deprotection in peptide chemistry and modern organic synthesis. Graphical Abstract: [Figure not available: see fulltext.]

Protection of carboxamide functions by the trityl residue. Application to peptide synthesis

Carboxamide functions may be tritylated by an acid-catalyzed reaction with triphenylmethanol and acetic anhydride in glacial acetic acid. The ω-trityl group of asparagine and glutamine is cleavable by TFA, but stable to strong mineral acids in aqueous solution, as well as to nucleophiles and bases. In peptide syntheses, it is ideally suited for combination with side-chain protections of the t.butyl-type.