62715-28-0

Basic information

• Product Name: H-HIS(1-TRT)-OME HCL
• Synonyms: N-IM-TRITYL-L-HISTIDINE METHYL ESTER HYDROCHLORIDE;N-TAU-TRITYL-HISTIDINE METHYL ESTER HYDROCHLORIDE;(S)-2-AMINO-3-(1-TRITYL-1H-IMIDAZOL-4-YL)-PROPIONIC ACID METHYL ESTER;HISTIDINE(1-TRT)-OME HCL;H-HIS(1-TRT)-OME HCL;H-HIS(T-TRT)-OME HCL;H-HIS(TRT)-OME HCL
• CAS NO: 62715-28-0
• Molecular Formula: C₂₆H₂₅N₃O₂
• Molecular Weight: 447.96
• Product Categories: Amino Acids and Derivatives;Amino Acid Derivatives
• Mol File: 62715-28-0.mol

Chemical Properties

• Boiling Point: 555.5±45.0 °C(Predicted)
• Appearance: /
• Density: 1.15±0.1 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 6.55±0.10(Predicted)
• CAS DataBase Reference: H-HIS(1-TRT)-OME HCL(CAS DataBase Reference)
• NIST Chemistry Reference: H-HIS(1-TRT)-OME HCL(62715-28-0)
• EPA Substance Registry System: H-HIS(1-TRT)-OME HCL(62715-28-0)

Safety Data

• Hazardous Substances Data: 62715-28-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-HIS(1-TRT)-OME HCL is used as a building block for the development of novel pharmaceutical compounds, leveraging its protective trityl group and modulatory methoxy group to facilitate the synthesis of complex peptide structures with enhanced properties.
Used in Peptide Synthesis:
In the field of peptide synthesis, H-HIS(1-TRT)-OME HCL serves as a key component, where its trityl protecting group ensures the selective protection of the histidine side chain during the assembly of peptide sequences, allowing for precise control over the synthesis process.
Used in Drug Development:
H-HIS(1-TRT)-OME HCL is utilized in drug development for the creation of new therapeutic agents, taking advantage of its modifiable hydrophobicity and solubility to design drugs with improved pharmacokinetics and pharmacodynamics.
Used in Chemical Research:
In chemical research, H-HIS(1-TRT)-OME HCL is employed as a model compound to study the effects of protecting groups and functional groups on the reactivity and properties of histidine-containing molecules, contributing to a deeper understanding of peptide chemistry and its applications.

Upstream product

• 40917-50-8 1,N^α-bis-benzyloxycarbonyl-histidine methyl ester 
• 76-83-5 trityl chloride 
• 4467-54-3 l-histidine methyl ester dihydrochloride 
• 937801-67-7 methyl-N^α-(((9H-fluoren-9-yl)methoxy)carbonyl)-N^τ-trityl-L-histidinate 
• 22888-57-9 2-(S)-(triphenylmethylamino)-3-<1-(triphenylmethyl)imidazol-4(5)-yl>propanoic acid methyl ester ditrityl-L-histidine methyl ester 
• 68262-63-5 N^α-benzyloxycarbonyl-N^im-triphenylmethyl-L-histidine methyl ester 
• 14997-58-1 N-[(benzyloxy)carbonyl]-L-histidine 
• 1499-46-3 L-Histidine methyl ester 
• 71-00-1 L-histidine 

Downstream Products

• 69937-82-2 (S)-2-{[1-Phenyl-meth-(E)-ylidene]-amino}-3-(1-trityl-1H-imidazol-4-yl)-propionic acid methyl ester 
• 937801-66-6 Fmoc-(His(Trt))2-OMe 
• 176752-35-5 methyl (2S)-2-(benzylamino)-3-[1-(triphenylmethyl)-1H-imidazol-4-yl]propanoate 

Relevant articles and documents

Self-healing response in supramolecular polymers based on reversible zinc-histidine interactions

Histidine-metal interactions are utilized in many biological materials as reinforcing crosslinks, and in particular, are believed to contribute as reversible crosslinks to the intrinsic self-recovery behavior of mussel byssal threads. In this contribution

Specifically and reversibly immobilizing proteins/enzymes to nitriolotriacetic-acid-modified mesoporous silicas through histidine tags for purification or catalysis

Six nitriolotriacetic-acid-modified ordered mesoporous silicas (NTA-OMPSs) with different pore sizes and surface features for specific and reversible protein immobilization were fabricated and characterized. Specific immobilization of a genetically engineered undecaprenyl pyrophosphate synthase (UPPs) from cell lysate and a chemically modified His-tagged horseradish peroxidase (HRP) in these Ni-NTA-OMPSs through histidine coordination to the nickelated NTA was demonstrated and confirmed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Negligible leakage of these enzymes over a wide range of acidic conditions was observed. Moreover, histidine tags with different lengths (His6, His4, His3, and His2) applied to HRP were evaluated to find the minimum length for effective complexation. Enzymatic assessment studies indicated that the pore size of the OMPSs has minimal influence on the enzymatic activity, whereas chemical entities such as unreacted mercapto groups tailored on the interior surfaces of the OMPSs played certain roles in inhibiting the enzymatic activity and stability. On MCF-S-NTA, SBA-S-NTA, and film-S-NTA, which contained unreacted mercaptopropyl groups on the interior surface, immobilized His-tagged HRP showed lower catalytic activity and stability than on MCF-NTA, film-NTA, and SBA-NTA. Selective hydroxylation of optically pure L-tyrosine to (S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid (L-DOPA) by the immobilized HRP was also demonstrated. Protein purification and enzyme catalysis: A generic and easily adaptable platform is established for selectively and reversibly immobilizing His-tagged enzymes in ordered mesoporous silicas (OMPSs) through nickelated nitriolotriacetic-acid (NTA)-histidine tag complexation (see figure). The immobilized enzymes exhibit good stability toward heat and pH changes. Negligible leakage of these enzymes over a wide range of acidic conditions was observed. Copyright

Synthesis and x-ray absorption spectroscopy structural studies of Cu(I) complexes of HistidylHistidine peptides: The predominance of linear 2-coordinate geometry

Modified His-His dipeptides have been reacted with copper(I) salts to model active-site Cu ions bound by contiguous His residues in certain oxygen-activating copper proteins, as well as amyloid β-peptide. Chelation of copper(I) by these ligands affords linear, two-coordinate complexes as studied structurally by X-ray absorption spectroscopy. The complexes are robust toward oxidation, showing limited to no reactivity with O2, and they bind CO weakly. Reaction with a third ligand (N-methylimidazole) affords complexes with a markedly different structure (distorted T-shaped) and reactivity, binding CO and oxidizing rapidly upon exposure to dioxygen. Copyright

Synthesis and evaluation of deglycobleomycin A2 analogues containing a tertiary N-methyl amide and simple ester replacement for the L-histidine secondary amide: Direct functional characterization of the requirement for secondary amide metal complexation

The synthesis and comparative examination of 3-5, analogues of deglycobleomycin A2 (2) which address the inferred importance of the L-histidine secondary amide directly, are detailed. The agent 3 lacks only the L-histidine β-hydroxy group of deglycobleomycin A2 and the corresponding agents 4 and 5 incorporate a tertiary N-methyl amide and simple ester in place of the L-histidine secondary amide. The DNA cleavage properties of 3 proved essentially indistinguishable from those of deglycobleomycin A2 (2) confirming that the distinctions between bleomycin A2 (1) and deglycobleomycin (2) are due to the removal of the disaccharide and not the introduction of the L-histidine free β-hydroxy group. The agents 4 and 5 containing a tertiary N-methyl amide and ester in place of the L-histidine secondary amide were found to cleave duplex DNA but to do so in a nonsequence selective fashion with a substantially reduced efficiency and a diminished double to single strand cleavage ratio that are only slightly greater than that of free iron itself. These latter observations establish the functional requirement for the L-histidine secondary amide and are consistent with the proposals that the L-histidine deprotonated secondary amide is required for functional metal chelation and activity.