7451-76-5

Basic information

• Product Name: diglycyl-histidine
• Synonyms: diglycyl-histidine;L-Histidine, N-(N-glycylglycyl)-;Nsc 334195;N-(N-Glycylglycyl)histidine;GGH
• CAS NO: 7451-76-5
• Molecular Formula: C10H15N5O4
• Molecular Weight: 269.26
• Mol File: 7451-76-5.mol
• Article Data: 2

Chemical Properties

• Melting Point: >210 °C (decomp)
• Boiling Point: 813.8±65.0 °C(Predicted)
• Appearance: /
• Density: 1.440
• Storage Temp.: ?20°C
• PKA: 2.82±0.10(Predicted)
• CAS DataBase Reference: diglycyl-histidine(CAS DataBase Reference)
• NIST Chemistry Reference: diglycyl-histidine(7451-76-5)
• EPA Substance Registry System: diglycyl-histidine(7451-76-5)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 7451-76-5(Hazardous Substances Data)

Usage

General Description

Diglycyl-histidine is a dipeptide compound composed of two amino acids, glycine and histidine, linked together through a peptide bond. It is often used as a chelating agent due to its ability to bind to metal ions, particularly copper and zinc. This makes it a valuable ingredient in metal chelation therapy, which is used to treat heavy metal poisoning and other metal-related health disorders. Additionally, diglycyl-histidine has been studied for its potential role as an antioxidant, as well as its ability to modulate the immune system and exert anti-inflammatory effects. Overall, diglycyl-histidine has promising potential as a therapeutic agent in the fields of metal toxicity and various inflammatory and oxidative stress-related conditions.

Upstream product

• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 116611-64-4 (9-fluorenylmethoxycarbonyl)-L-histidine 

Downstream Products

• 556-50-3 glycylglycine 
• 71-00-1 L-histidine 
• 2489-13-6 GH 
• 56-40-6 glycine 
• 53554-01-1 Cu(H-2 glycylglycyl-L-histidine)(1-) 

Relevant articles and documents

Utilizing reversible copper(II) peptide coordination in a sequence-selective luminescent receptor

Although vast information about the coordination ability of amino acids and peptides to metal ions is available, little use of this has been made in the rational design of selective peptide receptors. We have combined a copper(II) nitrilotriacetato (NTA) complex with an ammonium-ion-sensitive and luminescent benzocrown ether. This compound revealed micromolar affinities and selectivities for glycine- and histidine-containing sequences, which closely resembles those of copper(II) ion peptide binding: the two free coordination sites of the copper(II) NTA complex bind to imidazole and amido nitrogen atoms, replicating the initial coordination steps of non-complexed copper(II) ions. The benzocrown ether recognizes the N-terminal amino moiety intramolecularly, and the significantly increased emission intensity signals the binding event, because only if prior coordination of the peptide has taken place is the intramolecular ammonium ion-benzocrown ether interaction of sufficient strength in water to trigger an emission signal. Intermolecular ammonium ion-benzocrown ether binding is not observed. Isothermal titration calorimetry confirmed the binding constants derived from emission titrations. Thus, as deduced from peptide coordination studies, the combination of a truncated copper(II) coordination sphere and a luminescent benzocrown ether allows for the more rational design of sequence-selective peptide receptors.