TY - JOUR AU - Keszthelyi, Tamás AU - Holló, Gábor AU - Nyitrai, Gabriella AU - Kardos, Julianna AU - Héja, László TI - Bilayer Charge Reversal and Modification of Lipid Organization by Dendrimers as Observed by Sum-Frequency Vibrational Spectroscopy JF - LANGMUIR J2 - LANGMUIR VL - 31 PY - 2015 IS - 28 SP - 7815 EP - 7825 PG - 11 SN - 0743-7463 DO - 10.1021/acs.langmuir.5b00734 UR - https://m2.mtmt.hu/api/publication/2932290 ID - 2932290 N1 - Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, Budapest, H-1117, Hungary Institute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, Budapest, H-1117, Hungary Cited By :9 Export Date: 7 April 2021 CODEN: LANGD Correspondence Address: Keszthelyi, T.; Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, Hungary AB - Polyamidoamine (PAMAM) dendrimers are hyper-branched, nanosized polymers with promising biomedical applications as nanocarriers in targeted drug delivery and gene therapy. For the development of safe dendrimer-based biomedical applications it is necessary to gain an understanding of the detailed mechanism of the interactions of both cationic and anionic dendrimers with cell membranes. To characterize dendrimer membrane interactions we applied solid-supported lipid bilayers as biomembrane models and utilized infrared visible sum-frequency vibrational spectroscopy to independently probe the interactions of cationic G5-NH2 and anionic G4.5-COONa dendrimers with the two leaflets of the lipid bilayers. Interaction with both dendrimers led to changes in the interfacial water structure and charge density as evidenced by the changes in the OH band intensities in the sum-frequency spectra of the bilayers. Interaction with the G5-NH2 dendrimer also led to a unique inversion of the sign of the OH-stretch amplitudes, in addition to a decrease in their absolute values. We suggest that the positively charged amino groups on the G5-NH2 dendrimer surface bind to the negatively charged bilayer, while uncompensated positive charges not involved in the binding cause a reversal of the electric field and thus an opposite orientation of the interfacial water molecules. More subtle but nonetheless significant changes were seen in the relative magnitudes of the CH amplitudes. The methyl antisymmetric to symmetric stretch amplitude ratios are altered, implying changes in the tilt angles of the phospholipid alkyl chains. The conformational order of the phospholipid alkyl chains of both leaflets is also influenced by the G5-NH2 dendrimer while G4.5-COONa has no effect on the alkyl chain conformation. LA - English DB - MTMT ER -