Lipid-like behavior of signal sequence peptides at air-water interface

Biochimica et Biophysica Acta - Biomembranes

Volumn 1828, Issue 2, 2013, Pages 708-714

  Ambroggio, Ernesto E ^a   Fidelio, Gerardo D ^a  

^a UNIVERSIDAD NACIONAL DE CÓRDOBA   (Argentina)

Author keywords

Interfacial peptide structure; Lateral surface stability; Peptide monolayer; Peptide lipid interaction; PM IRRAS; Signal sequence peptide

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLCHOLINE; LIPID; PEPTIDE; SIGNAL PEPTIDE; SODIUM CHLORIDE; SYNTHETIC PEPTIDE; WATER;

ABSORPTION SPECTROSCOPY; AIR; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; COMPRESSION; INFRARED SPECTROSCOPY; LIPID MONOLAYER; MICELLE; MISCIBILITY; POLARIZED MODULATED INFRARED REFLECTION ABSORPTION SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; SURFACE PROPERTY;

AIR; AMINO ACID SEQUENCE; BIOPHYSICS; LIPIDS; MICELLES; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT; SODIUM CHLORIDE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SURFACE PROPERTIES; WATER;

EID: 84871797585     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.11.004     Document Type: Article

References (51)

1. L.M. Gierasch Signal sequences Biochemistry 28 1989 923 930
2. P. Walter, and A.E. Johnson Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane Annu. Rev. Cell Biol. 10 1994 87 119
3. G. von Heijne Transcending the impenetrable: how proteins come to terms with membranes Biochim. Biophys. Acta 947 1988 307 333
4. N. Zheng, and L.M. Gierasch Signal sequences: the same yet different Cell 86 1996 849 852
5. R.S. Hegde, and V.R. Lingappa Membrane protein biogenesis: regulated complexity at the endoplasmic reticulum Cell 91 1997 575 582
6. T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669
7. K.S. Matlin Spatial expression of the genome: the signal hypothesis at forty Nat. Rev. Mol. Cell Biol. 12 2011 333 340
8. G. Blobel, and D.D. Sabatini Ribosome-Membrane Interaction in Eukaryotic Cells L.A. Manson, Biomembranes vol. 2 1971 Plenum Publishing Corporation New York 193 195
9. T. Hainzl, S. Huang, G. Merilainen, K. Brannstrom, and A.E. Sauer-Eriksson Structural basis of signal-sequence recognition by the signal recognition particle Nat. Struct. Mol. Biol. 18 2011 389 391
10. B. Martoglio, and B. Dobberstein Signal sequences: more than just greasy peptides Trends Cell Biol. 8 1998 410 415
11. S. Jaud, M. Fernandez-Vidal, I. Nilsson, N.M. Meindl-Beinker, N.C. Hubner, D.J. Tobias, G. von Heijne, and S.H. White Insertion of short transmembrane helices by the Sec61 translocon Proc. Natl. Acad. Sci. U. S. A. 106 2009 11588 11593
12. A. Weihofen, K. Binns, M.K. Lemberg, K. Ashman, and B. Martoglio Identification of signal peptide peptidase, a presenilin-type aspartic protease Science 296 2002 2215 2218
13. B. Martoglio Intramembrane proteolysis and post-targeting functions of signal peptides Biochem. Soc. Trans. 31 2003 1243 1247
14. S.H. White Translocons, thermodynamics, and the folding of membrane proteins FEBS Lett. 555 2003 116 121
15. M. Bogdanov, and W. Dowhan Lipid-assisted protein folding J. Biol. Chem. 274 1999 36827 36830
16. R.C. Keller, J.A. Killian, and B. de Kruijff Anionic phospholipids are essential for alpha-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles Biochemistry 31 1992 1672 1677
17. T. Ahn, D.B. Oh, H. Kim, and C. Park The phase property of membrane phospholipids is affected by the functionality of signal peptides from the Escherichia coli ribose-binding protein J. Biol. Chem. 277 2002 26157 26162
18. T.J. McIntosh, A. Vidal, and S.A. Simon The energetics of binding of a signal peptide to lipid bilayers: the role of bilayer properties Biochem. Soc. Trans. 29 2001 594 598
19. G.D. Fidelio, B. Maggio, and F.A. Cumar Interaction of melittin with glycosphingolipids and phospholipids in mixed monolayers at different temperatures. Effect of the lipid physical state Biochim. Biophys. Acta 862 1986 49 56
20. E.E. Ambroggio, F. Separovic, J. Bowie, and G.D. Fidelio Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin Biochim. Biophys. Acta 1664 2004 31 37
21. E.E. Ambroggio, B. Austen, and G.D. Fidelio Biophysical properties of a synthetic transit peptide from wheat chloroplast ribulose 1,5-bisphosphate carboxylase J. Pept. Sci. 13 2007 245 252
22. E.E. Ambroggio, M.A. Villarreal, G.G. Montich, D.T. Rijkers, M.R. De Planque, F. Separovic, and G.D. Fidelio Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor Biophys. Chem. 121 2006 171 176
23. G.D. Fidelio, B.M. Austen, D. Chapman, and J.A. Lucy Properties of signal-sequence peptides at an air-water interface Biochem. J. 238 1986 301 304
24. V. Nolan, M. Perduca, H.L. Monaco, B. Maggio, and G.G. Montich Interactions of chicken liver basic fatty acid-binding protein with lipid membranes Biochim. Biophys. Acta 1611 2003 98 106
25. R.V. Vico, R.H. de Rossi, and B. Maggio PM-IRRAS assessment of the compression-mediated orientation of the nanocavity of a monoacylated beta-cyclodextrin in monolayers at the air-water interface Langmuir 26 2010 8407 8413
26. G.L. Gaines Insoluble Monolayers at Liquid-Gas Interfaces 1966 Interscience New York
27. K.S. Birdy Lipid and Biopolymers Monolayers at Liquid Interfaces 1989 Plenum Press New York
28. J.L. Arrondo, A. Muga, J. Castresana, and F.M. Goni Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy Prog. Biophys. Mol. Biol. 59 1993 23 56
29. G.L. Reddy, and R. Nagara Circular dichroism studies on synthetic signal peptides indicate beta-conformation as a common structural feature in highly hydrophobic environment J. Biol. Chem. 264 1989 16591 16597
30. A.M. Batenburg, R. Brasseur, J.M. Ruysschaert, G.J. van Scharrenburg, A.J. Slotboom, R.A. Demel, and B. de Kruijff Characterization of the interfacial behavior and structure of the signal sequence of Escherichia coli outer membrane pore protein PhoE J. Biol. Chem. 263 1988 4202 4207
31. B. Bechinger Structure and dynamics of the M13 coat signal sequence in membranes by multidimensional high-resolution and solid-state NMR spectroscopy Proteins 27 1997 481 492
32. V. Chupin, J.A. Killian, J. Breg, H.H. de Jongh, R. Boelens, R. Kaptein, and B. de Kruijff PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study Biochemistry 34 1995 11617 11624
33. Y. Yamamoto, T. Ohkubo, A. Kohara, T. Tanaka, and M. Kikuchi Conformational requirement of signal sequences functioning in yeast: circular dichroism and 1H nuclear magnetic resonance studies of synthetic peptides Biochemistry 29 1990 8998 9006
34. S.H. Portlock, Y. Lee, J.M. Tomich, and L.K. Tamm Insertion and folding of the amino-terminal amphiphilic signal sequences of the mannitol and glucitol permeases of Escherichia coli J. Biol. Chem. 267 1992 11017 11022
35. L.A. Correll, T.A. Woodford, J.D. Corbin, P.L. Mellon, and G.S. McKnight Functional characterization of cAMP-binding mutations in type I protein kinase J. Biol. Chem. 264 1989 16672 16678
36. C.J. McKnight, M.S. Briggs, and L.M. Gierasch Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties J. Biol. Chem. 264 1989 17293 17297
37. H. Raghuraman, and A. Chattopadhyay Effect of micellar charge on the conformation and dynamics of melittin Eur. Biophys. J. 33 2004 611 622
38. Z. Xu, J.W. Brauner, C.R. Flach, and R. Mendelsohn Orientation of peptides in aqueous monolayer films. Infrared reflection-absorption spectroscopy studies of a synthetic amphipathic beta-sheet Langmuir 20 2004 3730 3733
39. R. Mendelsohn, J.W. Brauner, and A. Gericke External Infrared Reflection Absorption Spectrometry of Monolayer Films at the Air-Water Interface Annu. Rev. Phys. Chem. 46 1995 305 334
40. G. Thakur, M. Micic, and R.M. Leblanc Surface chemistry of Alzheimer's disease: a Langmuir monolayer approach Colloids Surf. B Biointerfaces 74 2009 436 456
41. E.E. Ambroggio, D.H. Kim, F. Separovic, C.J. Barrow, K.J. Barnham, L.A. Bagatolli, and G.D. Fidelio Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide Biophys. J. 88 2005 2706 2713
42. R. Maget-Dana The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes Biochim. Biophys. Acta 1462 1999 109 140
43. R. Maget-Dana, D. Lelievre, and A. Brack Surface active properties of amphiphilic sequential isopeptides: Comparison between alpha-helical and beta-sheet conformations Biopolymers 49 1999 415 423
44. A. Wada The alpha-helix as an electric macro-dipole Adv. Biophys. 1976 1 63
45. W.G. Hol The role of the alpha-helix dipole in protein function and structure Prog. Biophys. Mol. Biol. 45 1985 149 195
46. W.G. Hol Effects of the alpha-helix dipole upon the functioning and structure of proteins and peptides Adv. Biophys. 19 1985 133 165
47. M.P. Caulfield, K. Park, M. Rosenblatt, and G.D. Fasman Correlation of secondary structure with biological activity for a leader peptide: circular dichroism-derived structure and in vitro biological activities of preproparathyroid hormone peptide and its analogs Arch. Biochem. Biophys. 289 1991 208 213
48. M.S. Briggs, D.G. Cornell, R.A. Dluhy, and L.M. Gierasch Conformations of signal peptides induced by lipids suggest initial steps in protein export Science 233 1986 206 208
49. S.W. Chi, G.S. Yi, J.Y. Suh, B.S. Choi, and H. Kim Structures of revertant signal sequences of Escherichia coli ribose binding protein Biophys. J. 69 1995 2703 2709
50. L. Voglino, T.J. McIntosh, and S.A. Simon Modulation of the binding of signal peptides to lipid bilayers by dipoles near the hydrocarbon-water interface Biochemistry 37 1998 12241 12252
51. D.G. Cornell, R.A. Dluhy, M.S. Briggs, C.J. McKnight, and L.M. Gierasch Conformations and orientations of a signal peptide interacting with phospholipid monolayers Biochemistry 28 1989 2789 2797