H-D-Ala-Gln-octadecyl ester hydrochloride (CAS 153508-74-8)

H-D-Ala-Gln-octadecyl ester hydrochloride is a dipeptide derivative where the amino acids D-alanine and glutamine are linked together, and the glutamine side chain is modified with an octadecyl ester. This modification introduces a long hydrophobic tail, making the molecule amphiphilic — a characteristic that has been exploited in various scientific research areas, particularly in the study of membrane biology and the design of peptide-based delivery systems. In scientific research, H-D-Ala-Gln-octadecyl ester hydrochloride has been used to investigate the mechanisms of peptide interaction with lipid bilayers. The hydrophobic octadecyl tail allows the molecule to insert into lipid membranes, making it an excellent probe for studying membrane dynamics, the formation of micelles, and the self-assembly of amphiphilic compounds. This compound helps in understanding how peptides can modulate membrane properties, including fluidity, phase behavior, and permeability. Moreover, this chemical has been utilized in the development of novel peptide-based delivery systems. Its amphiphilic nature enables the formation of stable nanostructures that can encapsulate hydrophobic drugs, facilitating their transport and delivery to targeted cells. Research using H-D-Ala-Gln-octadecyl ester hydrochloride has contributed to the design of nanocarriers that improve the solubility and bioavailability. Additionally, this compound has been used to study peptide-lipid interactions, which are crucial for the design of antimicrobial peptides and the understanding of their mechanisms of action. By analyzing how the hydrophobic tail interacts with bacterial membranes, researchers can gain insights into how to design more effective antimicrobial agents that can disrupt bacterial membrane integrity without the use of traditional antibiotics.