Interfacial Behaviors of Transmembrane Peptides in Lipid Bilayer Studied by X-Ray and Neutron Reflectivity

Abstract:

Lipids and proteins can influence each other in so many different ways. Lipids may affect the structure of membrane proteins by influencing their backbone conformation, the tilt, rotation angles of their transmembrane (TM) segments, and the orientation of their side chains. The membrane-spanning parts in integral membrane proteins are predominantly hydrophobic, and most often helical. At the lipid-protein interface, the TM part of the protein and the hydrocarbon chains of the lipid molecules have to coexist to maintain the integrity of the membrane. Lipids are important components of lipid membrane are used in various experiments reported in this thesis and can act as model lipid bilayers. Once they support on solid substrate like silicon wafers, their structural properties can investigate by X-ray and neutron reflectivity and by other useful techniques. Reflectivity technique can provide detailed information such as their thickness and interaction between lipids and peptides. The thesis reports a detailed investigation of these lipids and peptides by X-ray and neutron reflection techniques

• Periodical: Materials Science Forum (Volume 977)
• Pages: 184-189
• DOI: https://doi.org/10.4028/www.scientific.net/MSF.977.184
• Online since: February 2020
• Authors: Dong Jin Choi*, Zeeshan Ur Rehman
• Keywords: Lipid Bilayer, Neutron Reflectivity, Peptides, Transmemebrane, WALP, X-Ray

References

[1] Lee AG, How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta, vol. 1666, 62-87 (2004).

[2] Mcintosh TJ, Simon SA, Roles of bilyer material properties in function and distribution of membrane proteins, Annu Rev Biophys Biomol Struct, vol. 35, 177-198 (2006).

DOI: 10.1146/annurev.biophys.35.040405.102022

[3] De Planque MRR, Killian JA, Protein-lipid interactions studied with designed transmembrane peptides, role of hydrophobic matching and interfacial anchoring, Mol Membr Biol, vol. 20, 271-284 (2004).

DOI: 10.1080/09687680310001605352

[4] De Planque, M. R. R., D. V. Greathouse, R. E. Koeppe, II, H. Schäfer, D. Marsh, and J. A. Killian. Influence of lipid/peptide mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane a-helical peptides and gramicidin A. Biochemistry. vol. 37:9333–9345 (1998).

DOI: 10.1021/bi980233r

[5] De Planque, M. R. R., J. A. W. Kruijtzer, R. M. J. Liskamp, D. Marsh, D. V. Greathouse, R. E. Koeppe, II, B. de Kruijff, and J. A. Killian. Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane a-helical peptides. J. Biol. Chem. vol. 274, 20839–20846 (1999).

DOI: 10.1074/jbc.274.30.20839

[6] Killian, J. A., I. Salemink, M. R. R. de Planque, G. Lindblom, R. E. Koeppe, II, and D. V. Greathouse. Introduction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane a-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. vol. 35, 1037–1045 (1996).

DOI: 10.1021/bi9519258

[7] Morein, S., E. Strandberg, J. A. Killian, S. Persson, G. Arvidson, R. E. Koeppe, II, and G. Lindblom. Influence of membrane-spanning a-helical peptides on the phase behaviour of dioleoylphosphatidylcholine/water system. Biophys. J. vol. 73, 3078 –3088 (1997).

DOI: 10.1016/s0006-3495(97)78335-8

[8] Huschilt, J. C., R. S. Hodges, and J. H. Davis. Phase equilibria in an amphiphilic peptide-phospholipid model membrane by deuterium nuclear magnetic resonance difference spectroscopy. Biochemistry. vol. 24, 1377–1386 (1985).

DOI: 10.1021/bi00327a015

[9] Morrow, M. R., J. C. Huschilt, and J. H. Davis. Simultaneous modelling of phase and calorimetric behavior in an amphiphilic peptide/phospholipid model membrane. Biochemistry. vol. 24, 5396 –5406 (1985).

DOI: 10.1021/bi00341a018

[10] Zhang, Y.-P., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. Interaction of a peptide model of a hydrophobic transmembrane a-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetric and FTIR spectroscopic studies. Biochemistry. vol. 31, 11579 –11588 (1992).

DOI: 10.1021/bi00161a042

[11] Zhang, Y.-P., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 1995. Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers. Biochemistry. vol. 34:2362–2371.

DOI: 10.1021/bi00007a032

[12] A. O'Connell, R. Koeppe Ⅱ, and O. Andersen, Kinetics of gramicidin channel formation in lipid bilayer: Transmembrane monomer association,, Science, vol 250, pp.1256-1259 (1990).

DOI: 10.1126/science.1700867

[13] M. Schiffer, C. Chang, and F. Stevens, The functions of tryptophan residues in membrane proteins,, Protein Engr., vol. 5, pp.213-214 (1992).

[14] J. Killian, I. Salemik, M. dePlanque, G. Lindblom, R. Koeppe Ⅱ, and D. Greathouse, Introduction of nonbilayer structure in diacylphosphatidylcholin model membranes by transmembrane a-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophan,, Biochemistry, vol. 35, pp.1037-1045 (1996).

DOI: 10.1021/bi9519258

[15] P. van der Wel, T. Pott, S. Morein, D. Greathouse, R. Koeppe 2, and K. J.A., Tryptophan-anchored transmembrane peptides promote formation of nonlamelar phases in phosphatidylethanolamine model membranes in a mismatch-dependent manner, Biochemistry, vol. 39, 3124-3133 (2000).

DOI: 10.1021/bi9922594

[16] W. –M. Yau, W. Wimlay, K. Gawritsch, and S. White, The preference of tryptophan for membrane interfaces, Biochemistry, vol 37, 14713-14718 (1998).

DOI: 10.1021/bi980809c

[17] Maurits R. R. de Planque, Erik Goormaghtigh, Denise V. Greathouse, Roger E. Koeppe Ⅱ, John A. W. Kruijtzer, Rob M. J. Liskamp, Ben de Kruijff, and j. Antoinette Killian, 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. Biochemistry, vol 40, 5000-5010 (2001).

DOI: 10.1021/bi000804r

[18] Maurits R. R. de Planque, Boyan B. Nonev, Jerouen A. A. Demmers, Denise V. Greathouse, Roger E. Koeppe Ⅱ, Frances Separovic, Anthony Watts, and J. Antoinette Killian. Biochemistry, vol 42, 5341-5348 (2003).

DOI: 10.1021/bi027000r