200625-76-9

Basic information

• Product Name: H-D-GLN(TRT)-OH
• Synonyms: H-D-GLN(TRT)-OH;D-GLUTAMINE(TRT)-OH;N-GAMMA-TRITYL-D-GLUTAMINE;N-DELTA-TRITYL-D-GLUTAMINE;N-(Triphenylmethyl)-D-glutamine;D-Gln(Trt)-OH·H2O;Nd-Trityl-D-glutamine hydrate≥ 99% (HPLC)
• CAS NO: 200625-76-9
• Molecular Formula: C24H24N2O3
• Molecular Weight: 388.46
• Mol File: 200625-76-9.mol
• Article Data: 5

Chemical Properties

• Boiling Point: 658.003 °C at 760 mmHg
• Flash Point: 351.748 °C
• Appearance: /
• Density: 1.214 g/cm3
• Vapor Pressure: 0 mmHg at 25°C
• Storage Temp.: -15°C
• CAS DataBase Reference: H-D-GLN(TRT)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-D-GLN(TRT)-OH(200625-76-9)
• EPA Substance Registry System: H-D-GLN(TRT)-OH(200625-76-9)

Safety Data

• Hazardous Substances Data: 200625-76-9(Hazardous Substances Data)

Usage

General Description

H-D-GLN(TRT)-OH is a chemical compound with the molecular formula C23H27N3O5. It is a derivative of glutamine, an important amino acid that plays a crucial role in protein synthesis and serves as a source of energy for cells. The compound is commonly used in peptide synthesis and as a building block for creating peptide chains. H-D-GLN(TRT)-OH is a protected form of glutamine, with the TRT (trityl) group serving as a temporary protective agent for the amine group, allowing for selective deprotection and manipulation of the molecule during peptide synthesis. It is commonly used in the pharmaceutical and biotechnology industries for the production of peptide-based drugs and research purposes.

InChI:InChI=1S/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-/m1/s1

Upstream product

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

Downstream Products

• 1472653-60-3 (S)-2-azido-5-oxo-5-(tritylamino)pentanoic acid 
• 1638884-71-5 N_α-(phenoxycarbonyl)-N_δ-trityl-L-glutamine 
• 1438859-93-8 (S)-2-hydroxy-5-oxo-5-(tritylamino)pentanoic acid 
• 132388-65-9 Fmoc-Gln(Trt)-OPfp 
• 132388-63-7 Fmoc-Gln(trityl) 2,4,5-trichlorophenyl ester 
• 132388-69-3 Boc-L-Gln(Trt)-OH 

Relevant articles and documents

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.

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.