AC-HIS-HIS-GLY-HIS-OH

Product Name:AC-HIS-HIS-GLY-HIS-OH

Synonyms:(2S)-2-[[2-[[(2S)-2-[[(2S)-2-acetamido-3-(1H-imidazol-5-yl)propanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]acetyl]amino]-3-(1H-imidazol-5-yl)propanoic acid

CAS No:287399-97-7

Purity:95%

Molar Mass:528.5

Chemical Formula:C22H28N10O6

Storage:Store at -20 degrees Celsius

Sequence:HHGH

Application:

Ac-His-His-Gly-His-OH is a synthetic tetrapeptide, consisting of three histidine residues and one glycine, with an acetylated N-terminus and a free carboxyl group at the C-terminus. This peptide is designed for research purposes, particularly in studies related to metal ion binding due to the high affinity of histidine residues for metals like zinc, copper, and nickel. The sequence is often used in biochemistry and molecular biology to investigate protein interactions with metal ions, enzyme active sites, or as a model for histidine-rich peptides in metalloprotein studies. Ac-His-His-Gly-His-OH is a valuable tool for exploring the role of histidine in biological systems and metal coordination chemistry.

Current Research:

Ac-His-His-Gly-His-OH (CAS: 287399-97-7) is a synthetic tetrapeptide composed of the amino acids histidine and glycine, with an acetyl group capping the N-terminus and a free carboxyl group at the C-terminus. This peptide is notable for its histidine-rich sequence, which imparts significant metal-binding properties, making it a valuable subject in biochemical and biophysical research.
Research Applications:
Metal Ion Coordination Studies: The abundance of histidine residues in Ac-His-His-Gly-His-OH facilitates strong coordination with metal ions, particularly transition metals like copper(II). This characteristic is exploited to model and understand the behavior of metalloproteins and metalloenzymes, providing insights into their structural and functional dynamics.
Enzymatic Activity Modeling: Investigations into the peptide's interaction with metal ions have demonstrated its ability to mimic the activity of certain metalloenzymes. For instance, copper(II) complexes of Ac-His-His-Gly-His-OH have been shown to exhibit superoxide dismutase-like activity, serving as functional models for this critical antioxidant enzyme.
Peptide Modification Techniques: The specific sequence of Ac-His-His-Gly-His-OH has been utilized in developing selective N-terminal acylation methods for peptides and proteins. The presence of glycine and histidine residues at the N-terminus enables targeted chemical modifications, which are essential in the synthesis of peptide-based therapeutics and in the study of protein function.
Conclusion:
Ac-His-His-Gly-His-OH is a versatile peptide that serves as a crucial tool in the exploration of metal-peptide interactions and the development of peptide modification strategies. Its unique properties continue to contribute to advancements in understanding metalloprotein functions and in the innovation of peptide-based applications in biomedical research.

Reference:

Jancs??, A., Paksi, Z., Jakab, N., Gyurcsik, B., Rockenbauer, A., & Gajda, T. (2005). Solution chemical properties and catecholase-like activity of the copper (ii)?CAc-His-His-Gly-His-OH system, a relevant functional model for copper containing oxidases.?Dalton Transactions, (19), 3187-3194.