Probing membrane topology by high-resolution 1H-13C heteronuclear dipolar solid-state NMR spectroscopy

被引:27
作者
Lu, JX [1 ]
Damodaran, K [1 ]
Lorigan, GA [1 ]
机构
[1] Miami Univ, Dept Chem & Biochem, Oxford, OH 45056 USA
关键词
SAMMY; phospholipid bilayers (bicelles); biologically pertinent molecules; H-1-C-13 dipolar coupling; membrane topology;
D O I
10.1016/j.jmr.2005.09.006
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Membrane topology changes introduced by the association of biologically pertinent molecules with membranes were analyzed utilizing the H-1-C-13 heteronuclear dipolar solid-state NMR spectroscopy technique (SAMMY) on magnetically aligned phospholipid bilayers (bicelles). The phospholipids H-1-C-13 dipolar coupling profiles lipid motions at the headgroup, glycerol backbone, and the acyl chain region. The transmembrane segment of phospholamban, the antimicrobial peptide (KIGAKI)(3) and cholesterol were incorporated into the bicelles, respectively. The lipids H-1-C-13 dipolar coupling profiles exhibit different shifts in the dipolar coupling contour positions upon the addition of these molecules, demonstrating a variety of interaction mechanisms exist between the biological molecules and the membranes. The membrane topology changes revealed by the SAMMY pulse sequence provide a complete screening method for analyzing how these biologically active molecules interact with the membrane. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:283 / 287
页数:5
相关论文
共 20 条
[1]   A novel linear amphipathic β-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids [J].
Blazyk, J ;
Wiegand, R ;
Klein, J ;
Hammer, J ;
Epand, RM ;
Epand, RF ;
Maloy, WL ;
Kari, UP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (30) :27899-27906
[2]   Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy [J].
Dave, PC ;
Tiburu, EK ;
Damodaran, K ;
Lorigan, GA .
BIOPHYSICAL JOURNAL, 2004, 86 (03) :1564-1573
[3]   High-resolution NMR spectroscopy of membrane proteins in aligned bicelles [J].
De Angelis, AA ;
Nevzorov, AA ;
Park, SH ;
Howell, SC ;
Mrse, AA ;
Opella, SJ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (47) :15340-15341
[4]   Efficient solid-state NMR methods for measuring heteronuclear dipolar couplings in unoriented lipid membrane systems [J].
Dvinskikh, SV ;
Castro, V ;
Sandström, D .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2005, 7 (04) :607-613
[5]   Heteronuclear dipolar recoupling in liquid crystals and solids by PISEMA-type pulse sequences [J].
Dvinskikh, SV ;
Zimmermann, H ;
Maliniak, A ;
Sandström, D .
JOURNAL OF MAGNETIC RESONANCE, 2003, 164 (01) :165-170
[6]   SOME NEW DEVELOPMENTS IN SOLID-STATE NUCLEAR MAGNETIC-RESONANCE SPECTROSCOPIC STUDIES OF LIPIDS AND BIOLOGICAL-MEMBRANES, INCLUDING THE EFFECTS OF CHOLESTEROL IN MODEL AND NATURAL SYSTEMS [J].
FORBES, J ;
BOWERS, J ;
SHAN, X ;
MORAN, L ;
OLDFIELD, E ;
MOSCARELLO, MA .
JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS I, 1988, 84 :3821-3849
[7]   Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR [J].
Hong, M ;
Gross, JD ;
Griffin, RG .
JOURNAL OF PHYSICAL CHEMISTRY B, 1997, 101 (30) :5869-5874
[8]   Influence of tryptophan on lipid binding of linear amphipathic cationic antimicrobial peptides [J].
Jin, Y ;
Mozsolits, H ;
Hammer, J ;
Zmuda, E ;
Zhu, F ;
Zhang, Y ;
Aguilar, MI ;
Blazyk, J .
BIOCHEMISTRY, 2003, 42 (31) :9395-9405
[9]   Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes [J].
Lu, JX ;
Damodaran, K ;
Blazyk, J ;
Lorigan, GA .
BIOCHEMISTRY, 2005, 44 (30) :10208-10217
[10]   The effects of cholesterol on magnetically aligned phospholipid bilayers: a solid-state NMR and EPR spectroscopy study [J].
Lu, JX ;
Caporini, MA ;
Lorigan, GA .
JOURNAL OF MAGNETIC RESONANCE, 2004, 168 (01) :18-30