Strength of integration of transmembrane α-helical peptides in lipid bilayers as determined by atomic force spectroscopy

被引:32
作者
Ganchev, DN
Rijkers, DTS
Snel, MME
Killian, JA
de Kruijff, B [1 ]
机构
[1] Univ Utrecht, Dept Biochem Membranes, Fac Chem, Biomembrane Inst,Dept Condensed Matter & Interfac, Utrecht, Netherlands
[2] Univ Utrecht, Fac Pharmaceut Sci, Dept Med Chem, Utrecht, Netherlands
关键词
D O I
10.1021/bi048372y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this study we address the stability of integration of proteins in membranes. Using dynamic atomic force spectroscopy, we measured the strength of incorporation of peptides in lipid bilayers. The peptides model the transmembrane parts of alpha-helical proteins and were studied in both ordered peptide-rich and unordered peptide-poor bilayers. Using gold-coated AFM tips and thiolated peptides, we were able to observe force events which are related to the removal of single peptide molecules out of the bilayer. The data demonstrate that the peptides are very stably integrated into the bilayer and that single barriers within the investigated region of loading rates resist their removal. The distance between the ground state and the barrier for peptide removal was found to be 0.75 +/- 0.15 nm in different systems. This distance falls within the thickness of the interfacial layer of the bilayer. We conclude that the bilayer interface region plays an important role in stably anchoring transmembrane proteins into membranes.
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收藏
页码:14987 / 14993
页数:7
相关论文
共 22 条
[1]   Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring (Review) [J].
de Planque, MRR ;
Killian, JA .
MOLECULAR MEMBRANE BIOLOGY, 2003, 20 (04) :271-284
[2]   Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions [J].
de Planque, MRR ;
Bonev, BB ;
Demmers, JAA ;
Greathouse, DV ;
Koeppe, RE ;
Separovic, F ;
Watts, A ;
Killian, JA .
BIOCHEMISTRY, 2003, 42 (18) :5341-5348
[3]   Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer:: Effects on backbone structure, orientation, and extent of membrane incorporation [J].
de Planque, MRR ;
Goormaghtigh, E ;
Greathouse, DV ;
Koeppe, RE ;
Kruijtzer, JAW ;
Liskamp, RMJ ;
de Kruijff, B ;
Killian, JA .
BIOCHEMISTRY, 2001, 40 (16) :5000-5010
[4]   Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spectrometry [J].
Demmers, JAA ;
van Duijn, E ;
Haverkamp, J ;
Greathouse, DV ;
Koeppe, RE ;
Heck, AJR ;
Killian, JA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (37) :34501-34508
[5]   Differences in zero-force and force-driven kinetics of ligand dissociation from β-galactoside-specific proteins (plant and animal lectins, immunoglobulin G) monitored by plasmon resonance and dynamic single molecule force microscopy [J].
Dettmann, W ;
Grandbois, M ;
André, S ;
Benoit, M ;
Wehle, AK ;
Kaltner, H ;
Gabius, HJ ;
Gaub, HE .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2000, 383 (02) :157-170
[6]   Dynamic strength of molecular adhesion bonds [J].
Evans, E ;
Ritchie, K .
BIOPHYSICAL JOURNAL, 1997, 72 (04) :1541-1555
[7]   Dynamic strengths of molecular anchoring and material cohesion in fluid biomembranes [J].
Evans, E ;
Ludwig, F .
JOURNAL OF PHYSICS-CONDENSED MATTER, 2000, 12 (8A) :A315-A320
[8]  
Evans E, 1998, FARADAY DISCUSS, V111, P1
[9]   How strong is a covalent bond? [J].
Grandbois, M ;
Beyer, M ;
Rief, M ;
Clausen-Schaumann, H ;
Gaub, HE .
SCIENCE, 1999, 283 (5408) :1727-1730
[10]   QUANTIZED ADHESION DETECTED WITH THE ATOMIC FORCE MICROSCOPE [J].
HOH, JH ;
CLEVELAND, JP ;
PRATER, CB ;
REVEL, JP ;
HANSMA, PK .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1992, 114 (12) :4917-4918