科研之友
微信
新浪微博
Facebook
分享链接
摘要
High-sensitivity differential scanning calorimetry was utilized to examine whether lipids capable of forming an inverted nonlamellar hexagonal II (H(II)) phase can be deposited into nanoporous substrate-supported arrays. Particularly, we compare the thermotropic phase properties of nanoconfined unsaturated 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine lipid bilayers with unsupported dispersions to assess nanoconfinement effects, focusing on the lamellar fluid (L(alpha)) to H(II) phase transition. Experimental results provide direct and clear evidence for the formation of an H(II) phase upon both heating and cooling. However, a small shift in the L(alpha)/H(II) phase transition temperature, as well as an increase in the magnitude of the associated temperature hysteresis, was observed in the nanoporous substrate-supported system. Additionally, nanoconfinement effects on the interaction and location of the antimicrobial peptide gramicidin S (GS) with nanoporous substrate-supported cardiolipin bilayers were examined by Fourier transform infrared spectroscopy as a function of temperature and phospholipid phase state. Upon heating, GS molecules began to insert into nanoconfined, substrate-supported cardiolipin bilayers at lower temperatures relative to the gel/liquid-crystalline phase transition temperature than into unsupported bilayers. The reduction in the polarity and hydrogen-bonding potential environment of GS in the L(alpha) state suggests that GS is located at the polar/apolar interfacial region in both supported and unsupported cardiolipin bilayers and that the capacity of GS to interact with nanoporous substrate-supported cardiolipin bilayers was not significantly hindered by nanoconfinement. These studies further demonstrate the usefulness of supported lipid bilayers inside nanoporous substrates.
- 出版日期2007-6-19
