Hydrophobic laminin-related peptides: Synthesis and surface properties

The synthesis of hydrophobic peptide derivatives related to the laminin seq uence [YIGSRNH(2)] is described. Hydrophobicity is achieved by the attachme nt of decanoic, myristic, or stearic acids to the amino terminal end of the peptide. Moreover, a cholesterol residue was also introduced as succinimid oyl-cholesteryl moiety at the same position. These peptidic compounds are d esigned to be inserted into lipid bilayers to prepare, what can be consider ed as, immunoliposomes to target these vesicles to tumor cells. Physicochem ical 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 derivat ive. The results obtained indicate that these peptide derivatives show a hi gh tendency to form aggregates in aqueous media, this fact reducing their i nteraction with lipid mono- and bilayers. The most suitable derivatives for interacting with liposomes are myristoyl and decanoyl. (C) 2001 Academic P ress.