Interaction of Lactoferrin and Its Peptides with DPPC and DPPG Liposomes Studied by Raman Spectroscopy
ZHANG Wei1, REN Fa-zheng1, GE Shao-yang1, 2, ZHANG Lu-da3, JIANG Lu1, MAO Xue-ying1, GUO Hui-yuan1*
1. College of Food Science & Nutritional Engineering, China Agricultural University, Key Laboratory of Functional Dairy, Ministry of Education，Beijing 100083, China 2. Beijing Higher Institution Engineering Research Center of Animal Product, Beijing 100083, China 3. College of Science, China Agricultural University, Beijing 100094, China
Abstract：Interaction of lactoferrin and its peptides LfcinB4-14 and LfampinB with dipalmitoylglycero-phosphocholine (DPPC) and dipalmitoylglycero-phosphoglycerol (DPPG) liposomes were studied by means of Raman spectroscopy. In our study, conformational changes in the phospholipid molecules were investigated by measuring the intensities of 2 847 and 2 882 cm-1 Raman bands which are assigned to acyl chains’ symmetric and asymmetric C—H stretching vibrations. The addition of lactoferrin and its peptides LfcinB4-14 and LfampinB caused a decrease in the 2 882 cm-1 intensity of DPPG liposomes, thus the order parameter for the lateral interactions between chains Slat decreased from 0.19 to 0.17, 0.14 and 0.12 respectively. On the contrary, the intensities at 2 847 and 2 882 cm-1 of DPPC liposomes were poorly affected by lactoferrin and its peptides. The results show that lactoferrin and its peptides present a stronger effect on the molecular structure and order degree of anionic lipid DPPG than that of zwitterionic lipid DPPC. This suggests that lactoferrin, LfcinB4-14 and LfampinB can interact and combine with the negatively charged DPPG liposomes by electrostatic interaction and perform its antibacterial activity. Besides, LfcinB4-14 and LfampinB can affect the lipid more strongly than lactoferrin.
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