The chemical substance "Ac-His-His-Gly-His-OH," with the CAS number 287399-97-7, is a peptide that consists of a sequence of amino acids, specifically histidine (His) and glycine (Gly), with an acetyl (Ac) group at the N-terminus and a hydroxyl (OH) group at the C-terminus. This peptide is characterized by its potential to participate in various biochemical interactions due to the presence of histidine residues, which can coordinate metal ions and play a role in enzyme catalysis. The acetylation at the N-terminus can enhance the peptide's stability and bioavailability, while the hydroxyl group at the C-terminus may influence its solubility and interaction with other biomolecules. Peptides like Ac-His-His-Gly-His-OH are often studied for their roles in biological systems, including their function in signaling pathways and their potential therapeutic applications. Overall, this compound exemplifies the complexity and functionality of peptides in biochemistry.

Ac-His-His-Gly-His-OH

287399-97-7: The chemical substance "Ac-His-His-Gly-His-OH," with the CAS number 287399-97-7, is a peptide that consists of a sequence of amino acids, specifically histidine (His) and glycine (Gly), with an acetyl (Ac) group at the N-terminus and a hydroxyl (OH) group at the C-terminus. This peptide is characterized by its potential to participate in various biochemical interactions due to the presence of histidine residues, which can coordinate metal ions and play a role in enzyme catalysis. The acetylation at the N-terminus can enhance the peptide's stability and bioavailability, while the hydroxyl group at the C-terminus may influence its solubility and interaction with other biomolecules. Peptides like Ac-His-His-Gly-His-OH are often studied for their roles in biological systems, including their function in signaling pathways and their potential therapeutic applications. Overall, this compound exemplifies the complexity and functionality of peptides in biochemistry.

<p>Ac-His-His-Gly-His-OH is a lysine ligand with an acetyl group and two histidine residues. Acetylation of the hydroxyl group on the lysine residue is necessary for binding to metal ions, such as protonation. This molecule has been shown to have five different protonation states at neutral pH. The protonated form has been found to be more soluble in water than the deprotonated form. Acetylation of both lysines in the molecule leads to hydrolytic cleavage of the amide bond, which causes it to become insoluble in water. Acetylation also alters chemical properties, such as changes in color; for example, this molecule exhibits dichroism when viewed under polarized light.</p>

CAS 287399-97-7

Ac-His-His-Gly-His-OH

Ac-His-His-Gly-His-OH

Ref: 3D-FA108490