Hydrophobic Laminin-Related Peptides: Synthesis and Surface Properties

• Published in: Journal of colloid and interface science Vol. 239; no. 1; pp. 64 - 70
• Main Authors: Reig, Francesca, Haro, Isabel, Polo, Dolores, Sospedra, Patricia, Alsina, M.Asunción
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 01-07-2001; Elsevier
• Subjects: Biological and medical sciences; delivery systems; fluorescence; General pharmacology; liposomes; Medical sciences; peptide synthesis; Pharmaceutical technology. Pharmaceutical industry; Pharmacology. Drug treatments; surface activity; targeting; surface activity; targeting; delivery systems; liposomes; fluorescence; peptide synthesis; Laminin; Pharmaceutical technology; Targeting; Peptides; Controlled release form; Dosage form; Liposome; Drug carrier; Hydrophobicity; Chemical synthesis; Physicochemical properties
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1006/jcis.2001.7528

The synthesis of hydrophobic peptide derivatives related to the laminin sequence [YIGSRNH2] is described. Hydrophobicity is achieved by the attachment of decanoic, myristic, or stearic acids to the amino terminal end of the peptide. Moreover, a cholesterol residue was also introduced as succinimidoyl-cholesteryl moiety at the same position. These peptidic compounds are designed to be inserted into lipid bilayers to prepare, what can be considered as, immunoliposomes to target these vesicles to tumor cells. Physicochemical aspects related to their surface activity, insertion into lipid layers, spreadibility, formation of aggregates, and haemolytic activity have been studied as a previous step in the selection of the most convenient derivative. The results obtained indicate that these peptide derivatives show a high tendency to form aggregates in aqueous media, this fact reducing their interaction with lipid mono- and bilayers. The most suitable derivatives for interacting with liposomes are myristoyl and decanoyl.