Abstract
Peptide YIGSR from the β1 chain of laminin promotes cell adhesion, migration, inhibits angiogenesis and tumor metastasis. Properties of YIGSR and a mutated sequence LIGSR in Langmuir films interacting with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) and in vesicles are presented in this work. The mixed lipid–peptide systems have been characterized 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.
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