Dyck Martina, Kerth Andreas, Blume Alfred, Lösche Mathias
University of Leipzig, Institute of Experimental Physics I, D-04103 Leipzig, Germany.
J Phys Chem B. 2006 Nov 9;110(44):22152-9. doi: 10.1021/jp062537q.
The association of neuropeptide Y (NPY) at the air/water interface and with phospholipid monolayers on water as subphase has been investigated using external infrared reflection absorption spectroscopy (IRRAS). Studies of the conformation and orientation of NPY suggest that it adopts an alpha-helical structure and is oriented parallel to the air/water interface in neat peptide monolayers. Both secondary structure and orientation are preserved in mixed lipid/NPY monolayers. Comparison of NPY associated with zwitterionic DPPC and with anionic DMPS suggests that electrostatic attraction plays a major role for peptide binding to the membrane surface.
利用外部红外反射吸收光谱法(IRRAS)研究了神经肽Y(NPY)在空气/水界面以及以水为亚相的磷脂单层上的情况。对NPY的构象和取向的研究表明,它呈现α-螺旋结构,并且在纯肽单层中与空气/水界面平行取向。二级结构和取向在脂质/NPY混合单层中均得以保留。将与两性离子DPPC和阴离子DMPS相关联的NPY进行比较表明,静电吸引在肽与膜表面的结合中起主要作用。