메뉴 건너뛰기




Volumn 4, Issue 1, 1994, Pages 79-86

Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE;

EID: 0028013531     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(94)90063-9     Document Type: Article
Times cited : (171)

References (76)
  • 2
    • 0026447586 scopus 로고
    • Crystal Structures of membrane lipids
    • of outstanding interest, This is a systematic and thorough review of the structures of membrane lipids determined by X-ray crystallography.
    • (1992) Biochim Biophys Acta , vol.1113 , pp. 339-373
    • Pascher1    Lundmark2    Nyholm3    Sundell4
  • 3
    • 0026011502 scopus 로고
    • Fluid Bilayer Structure Determination by the Combined use of X-Ray and Neutron Diffraction. 1. Fluid Bilayer Models and the Limits of Resolution
    • of outstanding interest, This paper addresses the fundamental issues regarding the determination of the structure of fluid bilayers.
    • (1991) Biophys J , vol.59 , pp. 162-173
    • Wiener1    White2
  • 4
    • 0023111150 scopus 로고
    • Determination of the Depth of Bromine Atoms in Bilayers Formed from Bromolipid Probes
    • (1978) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh1    Holloway2
  • 5
    • 0018280201 scopus 로고
    • A Direct Method for Determination of Membrane Electron Density Profiles on an Absolute Scale
    • (1978) Nature , vol.276 , pp. 530-532
    • Franks1    Arunachalam2    Caspi3
  • 6
    • 0025819980 scopus 로고
    • The Transbilayer Distribution of Bromine in Fluid Bilayers Containing a Specifically Brominated Analog of Dioleoylphosphatidylcholine
    • (1991) Biochemistry , vol.30 , pp. 6997-7008
    • Wiener1    White2
  • 7
    • 0017232478 scopus 로고
    • Structural Analysis of Hydrated Egg Lecithin and Cholesterol Bilayers. II. Neutron Diffraction
    • (1976) J Mol Biol , vol.100 , pp. 359-378
    • Worcester1    Franks2
  • 9
    • 0026048378 scopus 로고
    • The Structure of a Fluid Dioleoylphosphatidylcholine Bilayer Determined by Joint Refinement of X-Ray and Neutron Diffraction Data I Scaling of Neutron Data and the Distribution of Double-Bonds and Water
    • (1991) Biophysical Journal , vol.60 , pp. 508-576
    • Wiener1    King2    White3
  • 10
    • 0025964363 scopus 로고
    • Fluid Bilayer Structure De-termination by the Combined use of X-Ray and Neutron Diffraction. II. “Composition space” refinement method
    • •u] above and describes the fundamental principles of the refinement method.
    • (1991) Biophys J , vol.59 , pp. 174-185
    • Wiener1    King2    White3
  • 11
    • 0026683431 scopus 로고
    • Structure of a Fluid Dioleoylphosphaidylcholine Bilayer Determined by Joint Refinement of X-Ray and Neutron Diffraction Data. II. Distribution and Packing of Terminal Methyl Groups
    • (1992) Biophys J , vol.61 , pp. 428-433
    • Wiener1    White2
  • 12
    • 0026729232 scopus 로고
    • Structure of a Fluid Dioleoylphos phatidylcholine Bilayer Determined by Joint Refinement of X-Ray and Neutron Diffraction Data. III. Complete Structure
    • of outstanding interest, This paper presents the fully resolved image of a fluid bilayer, an analysis of the experimental uncertainties, and a comparison of the results with those from more traditional bilayer diffraction studies.
    • (1992) Biophys J , vol.61 , pp. 434-447
    • Wiener1    White2
  • 13
    • 0017752553 scopus 로고
    • Deuterium Magnetic Resonance: Theory and Application to Lipid Membranes
    • (1977) Q Rev Biophys , vol.10 , pp. 353-418
    • Seelig1
  • 14
    • 0019496872 scopus 로고
    • Location of Hexane in Lipid Bilayers Determined by Neutron Diffraction
    • (1981) Nature , vol.290 , pp. 161-163
    • White1    King2    Cain3
  • 19
  • 20
    • 0027177537 scopus 로고
    • Langevin Dynamics Studies of Unsaturated Phospholipids in a Membrane Environment
    • (1993) Biophys J. , vol.65 , pp. 1084-1092
    • Pearce1    Harvey2
  • 21
    • 0019464222 scopus 로고
    • The Spontaneous Insertion of Proteins Into and Across Membranes: The Helical Hairpin Hypothesis
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman1    Steiz2
  • 22
    • 0024558250 scopus 로고
    • The Nature of the Hydrophobic Binding of Small Peptides at the Bilayer Interface: Implications for the Insertion of Transbilayer Helices
    • of outstanding interest, The five questions addressed in this review evolved from work presented in this paper. It describes the results of thermodynamic measurements of the binding of tripeptides to bilayers and neutron diffraction measurements of their location. The importance of the bilayer interfacial regions in peptide binding and secondary structure formation is stressed.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs1    White2
  • 23
    • 0023043189 scopus 로고
    • Mixtures of a Scrires of Homologous Hydrophobic Peptides with Lipid Bilayers: A Simple Model System for Examining the Protein-Lipid Interface
    • (1986) Biochemtry , vol.25 , pp. 2605-2611
    • Jacobs1    White2
  • 24
    • 0023662574 scopus 로고
    • Lipid Bylaycr Perturbations Induced by Simple Hydrophobic Peptides
    • (1987) Biochemistry , vol.26 , pp. 6127-6134
    • Jacobs1    White2
  • 25
    • 0000483613 scopus 로고
    • 1H NMR Study
    • of outstanding interest, This is an important extension to the work of Jacobs and White [23] that fills in many details regarding the disposition of the tripeptides in the interface and the changes in peptide conformation rhat accompany partitioning.
    • (1993) J Phys Cbem , vol.97 , pp. 2967-2973
    • Brown1    Huestis2
  • 27
    • 0024968216 scopus 로고
    • Orientation of AlphaHelical Peptides in a Lipid Bilayer
    • of special interest, This paper provides the first direct structural evidence that a model hydrophobic α-helix spans lipid bilayers.
    • (1989) Biochim Biophys Acta , vol.979 , pp. 139-141
    • Huschilt1    Millman2    Davis3
  • 28
    • 0027459169 scopus 로고
    • X-Ray Scattering with Momentum Transfer in the Plane of Membrane: Application to Gramicidin Organization
    • (1993) Biophys J , vol.64 , pp. 157-162
    • He1    Ludtke2    Wu3    Huang4
  • 29
    • 0025889072 scopus 로고
    • Lipid-Alamcthicin Interactions Influence Alamethicin Orientation
    • of special interest, The most important observation is that hydration affects the orientation of alamethicin in the bilayer. It demonstrates the usefulness of oriented circular dichroism.
    • (1991) Biophys J , vol.60 , pp. 1079-1087
    • Huang1    Wu2
  • 30
  • 31
    • 0025993413 scopus 로고
    • Orientation of Melittin in Phospholipid Bilayers — A Polarized Attenuated Total Reflection Infrared Study
    • of special interest, This paper, like that of Huang and Wu [2901] demonstrates the effect of hydraton on the orientation of the helical peptide in the bilayer.
    • (1991) Biophys J , vol.60 , pp. 922-930
    • Frey1    Tamm2
  • 32
    • 0027484593 scopus 로고
    • Orientation of Fusion Active Synthetic Peptides in Phospholipid Bilayers: Determination by Fourier Transform Infrared Spectroscopy
    • (1993) Biochemistry , vol.32 , pp. 9729-9797
    • Ishiguro1    Kimura2    Takagashi3
  • 33
    • 0025051457 scopus 로고
    • Quenching of Tryptophan Fluoresence by Brominated Phospholipid
    • of special interest, Quenching of tryptophan fluoresence is used to demonstrate that a synthetic hydrophobic peptide spans the lipid bilayer.
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen1    Holloway2
  • 34
    • 0026721333 scopus 로고
    • Fluorescence Studies of the Secondary Structure and Orientation of a Model Ion Channel Peptide in Phospholipid Vesicles
    • of special interest, Here, quenching of tryptophan fluoresence is used to demonstrate that a helical synthetic peptide lies parallel to the bilayer plane.
    • (1992) Biochemistry , vol.31 , pp. 6608-6616
    • Chung1    Lear2    Degrado3
  • 35
    • 0026434565 scopus 로고
    • NMR Studies of the Structure and Dynamics of Membrane-Bound Bacteriophage Pfl Coat Protein
    • of special interest, The conformation of a natural peptide in micelles and bilayrers was determined using two- and three-dimensional NMR methodology. It shows that the peptide has two helical domains; one domain spans the bilayer while the other lies parallel to the bilyer interface.
    • (1991) Science , vol.252 , pp. 1303-1304
    • Shon1    Kim2    Colnago3    Opella4
  • 36
    • 0027447891 scopus 로고
    • Colicin E1 Binding to Membranes: Time-Resolved Studies of Spin-Labeled Mutants
    • of special interest, Although the work primarily concerns the mechanism of the insertion of colicin E1 into membranes, the methods described should be useful for studying the incorporation of synthetic peptides into bilayers.
    • (1993) Science , vol.259 , pp. 960-963
    • Shin1    Levinthal2    Levinthal3    Hubbell4
  • 37
    • 0027360175 scopus 로고
    • High-Resolution Conformation of Gramicidin A in a Lipid Bilayer by Solid-State NMR
    • of outstanding interest, This elegant work lays the foundation for the use of solid state NMR for the determination of peptide structures in oriented lipid multilayers.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem1    Ho2    Cross3
  • 38
    • 0026442901 scopus 로고
    • Interaction of a Peptide Model of a Hydrophobic Transmembrane Alpha-Helical Segment of a Membrane Protein with Phosphatidylcholine Bilayers: Differential Scanning Calorimetric and MR Spectroscopic Studies
    • (1992) Biochemistry , vol.31 , pp. 11579-11588
    • Zhang1    Lewis2    Hodges3    McElhaney4
  • 40
    • 0000589227 scopus 로고
    • Partitioning of Nonpolar Solutes Into Bilayers and Amorphous Normal-Alkanes
    • of outstanding of, This is a carefully executed study of the partitioning of hexane into bilayer and alkane phases. The results demonstrate how strongly the choice of partition coefficient units affect the solvation parameter used for calculating the free energy of transfer based upon acessible surface area. The paper also demonstrates that the surface density of the lipids in bilayers is a major determinant of hexane solubility.
    • (1990) J Phys Cbem , vol.94 , pp. 801-809
    • De Young1    Dill2
  • 41
    • 0026076664 scopus 로고
    • Extractng Hydrophobic Free Energies from Experimental Data: Relationship to Protein Folding and Theoretical Models
    • of outstanding interest, This paper, although controversial, makes a very strong case for the use of Flory-Huggins-corrected volume-fraction units for calculating free energies of transfer in partitioning experiments. The theoretical issues are discussed in detail.
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp1    Nicholls2    Friedman3    Honig4
  • 44
    • 0026881105 scopus 로고
    • The Use of Flory-Huggins Theory in Interpreting Partitioning of Solutes Between Organic Liquids and Water
    • ⊎⊎] that reveals the controversial nature of the analysis.
    • (1992) Biopolymers , vol.32 , pp. 711-715
    • Holtzer1
  • 46
    • 0025887899 scopus 로고
    • The Effect of a Membrane Potential on the Interaction of Mastoparan X, a Mitochondrial Presequence. and Several Regulatory Peptides with Phospholipid Vesicles
    • (1991) Biocbim Biophys Acta , vol.1068 , pp. 111-124
    • De Kroon1    De Grier2    De Kruijff3
  • 47
    • 0024503511 scopus 로고
    • Membrane Incorporation and Induction of Secondary Structure of Synthetic Peptides Corresponding to the N-Terminal Signal Sequences of the Glucocorticoid and Mannitol Permeases of Echerichia coli
    • (1989) J Biol Cbem , vol.264 , pp. 2587-2592
    • Tamm1    Tomich2    Saier3
  • 48
    • 0026702177 scopus 로고
    • Insertion and Folding of the Amino-Terminal Amphiphilic Signal Sequences of the Mannitol and Glucitol Permeases of Escherichia coli
    • (1992) J Biol Cbem , vol.267 , pp. 11017-11022
    • Portlock1    Lee2    Tomich3    Tamm4
  • 49
    • 0023654706 scopus 로고
    • Membrane Binding and Conformational Properties of Peptides Representing the NH2 Terminus if Influenza HA-2
    • (1987) J Biol Cbem , vol.262 , pp. 6500-6505
    • Lear1    Degrado2
  • 50
    • 0025182226 scopus 로고
    • The role of Charge and Hydrophobicity in Peptide Lipid Interaction — A Comparative Study Based on Tryptophan Fluoresence Measurements Combined with the Use of Aqueous and Hydrophobic Quenchers
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon1    Soekarjo2    De Gier3    De Kruiff4
  • 51
    • 0024328774 scopus 로고
    • Interaction of Melittin with Phosphatidylcholine Membranes. Binding Isotherm and Lipid Head-Group Conformation
    • (1989) Biochemistry , vol.28 , pp. 4216-4221
    • Kuchinka1    Seelig2
  • 54
    • 0025649676 scopus 로고
    • Peptide Binding to Lipid Bilayers — Binding Isotherms and Zeta-Potential of a Cyclic Somato statin Analogue
    • (1990) Biochemistry , vol.29 , pp. 10995-11000
    • Beschiaschviu1    Seelig2
  • 55
    • 0024571766 scopus 로고
    • Binding of a Neuropeptide, Substance P, to Neutral and Negatively Charged Lipids
    • (1989) Biocbemistry , vol.28 , pp. 2490-2496
    • Seelig1    McDonald2
  • 56
    • 0026507986 scopus 로고
    • Interaction of a Substance P Agonist and of Substance P Antagonists with Lipid Membranes. A Thermodynamic Analysis
    • (1992) Biochemistry , vol.31 , pp. 2897-2904
    • Seelig1
  • 57
    • 0025647096 scopus 로고
    • Membrane Insertion and Lateral Diffusion of Fluoresence-Labelled Cytochromec Oxidase SubunitIV Signal Peptide in Charged and Uncharged Phospholipid Bilayers
    • (1990) Biocbim J , vol.272 , pp. 713-719
    • Frey1    Tamm2
  • 59
    • 0027170648 scopus 로고
    • Membrane Partitioning Distinguishing Bilayer Effects from the Hydrophobic Effect
    • ⊎⊎ on the free energy of partitioning.
    • (1993) Biochemistry , vol.25 , pp. 6307-6313
    • Wimley1    White2
  • 62
    • 0015528115 scopus 로고
    • Interactions of Phosphatidylcholine Vesicles with 2-p-Toluidinylnaphthalene-6-Sulfonate
    • (1972) Biochemistry , vol.11 , pp. 735-740
    • Huang1    Charlton2
  • 63
    • 0027053107 scopus 로고
    • Partitioning of Tryptophan Side-Chain Analogs Between Water and Cyclohexane
    • (1992) Biochemistry , vol.31 , pp. 12813-12818
    • Wimley1    White2
  • 64
    • 0026808783 scopus 로고
    • Peptide Binding to Lipid Bilayers: Nonclassical Hydrophobic Effect and Membrane-Induced pK Shifts
    • ⊎⊎] is shown to be a feature of the partitioning of peptides into bilayers. An important conclusion is tthat the curvature of the vesicles affects the magnitude of the effect and thereby demonstrates how strongly changes in the packing of lipids in bilayers affect the thermodynamic parameters of partitioning.
    • (1992) Biochemistry , vol.31 , pp. 10044-10053
    • Beschiaschvili1    Seelig2
  • 65
    • 0025914405 scopus 로고
    • Binding of Peptides with Basic Residues to Membranes Containing Acidic Phospholipids
    • ⊎] provide an important foundation for understanding electrostatic interactions in the association of peptides with bilayers.
    • (1991) Biophys J , vol.60 , pp. 135-148
    • Kim1    Mosior2    Chung3    Wu4    McLaughlin5
  • 66
    • 0025789799 scopus 로고
    • Interaction of Charged and Uncharged Calcium Channel Antagonists with Phospholipid Membranes — Binding Equilibrium, Binding Enthalpy, and Membrane Location
    • ⊎] above.
    • (1991) Biochemistry , vol.30 , pp. 7203-7211
    • Bauerle1    Seelig2
  • 67
    • 0026572082 scopus 로고
    • Binding of Basic Peptides to Acidic Lipids in Membranes — Effects of Inserting Alanine(s) Between the Basic Residues
    • ⊎] above.
    • (1992) Biochemistry , vol.31 , pp. 1767-1773
    • Mosir1    McLaughlin2
  • 70
    • 0027525276 scopus 로고
    • Electrostatic and Nonpolar Peptide — Membrane Interactions. Lipid Binding and Functional Properties of Somatostatin Analogues of Charge z=+1 to Z=+3
    • ⊎ above.
    • (1993) Biochemistry , vol.32 , pp. 9714-9721
    • Seelig1    Nebel2    Ganz3    Bruns4
  • 72
    • 0000433840 scopus 로고
    • Surface-Induced Enhancement of Internal Structure in Polymers and Proteins
    • ⊎ use exhaustive enumeration of polymers on two- and three-dimensional lattices to explore in considerable detail the fundamental principles underlying the induction of secondary structure in polymers associated with interfaces.
    • (1990) J Chem Phys , vol.93 , pp. 8343-8351
    • Wattenbarger1    Chan2    Evans3    Bloomfield4    Dill5
  • 75
    • 0026661869 scopus 로고
    • Spontaneous Insertion of Polypeptide Chains into Membranes: A Monte-Carlo Model
    • of outstanding interest, The use of so-called off-lattice calculations for modeling the insertion of helical peptides into bilayers is described. This approach provides a useful way of examining the effect of hydrophobicity on insertion.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9391-9395
    • Milik1    Skolnick2
  • 76
    • 0027390459 scopus 로고
    • Insertion of Peptide Chains into Lipid Membranes: An Off-Lattice Montc-Carlo Dynamics Model
    • ⊎] are used as a starting point for the modeling presented in both papers.
    • (1993) Protein Struct Funct Genet , vol.15 , pp. 10-25
    • Milik1    Skolnick2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.