Interactions of laminin peptides with phospholipids in Langmuir films and vesicles

Properties of mixed films of laminin peptide YIGSR and a mutated sequence LIGSR with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) vesicles are have been studied using circular dichroic spectroscopy, quartz crystal microbalance and Brewster angle microscopic studies. LIGSR peptide seems to adhere strongly to POPC resulting in better organized lipid-peptide layer compared with the native YIGSR. The results suggest that even single amino acid mutations in such short sequences may be used to fine tune properties of the peptide.