Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes:  Infrared Spectroscopic Characterization at the Air/Water Interface

Dyck, Martina; Kerth, Andreas; Blume, and Alfred; Lösche, Mathias

doi:10.1021/jp062537q

Cited by 46 publications

(47 citation statements)

References 33 publications

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“…[24] When there is only a small amount of the peptide inside mixed lipid/peptide monolayers, the peptide is a-helical, while at higher peptide molar fraction it aggregates into b-sheets. The binding of Ras proteins through a membrane anchor [25] and the interaction of neuropeptide Y with lipid monolayers [26] have been investigated, and no secondary structure change was found. The "unusual" peptide dicynthaurin has been shown to incorporate into anionic DPPG monolayers without changes in secondary structure.…”

Section: Introductionmentioning

confidence: 99%

“…An increase in the intensity of the OH stretching band would indicate a peripheral adsorption of the peptide to the monolayer headgroup region due to a change in film thickness. [23,26] That this was not observed indicates that the thickness of the film changes only slightly, because the peptide molecules are inter- [16] and the peptide dicynthaurin, [27] which increase the surface pressure in DPPG monolayers by about 6-8 mNm À1 starting from a surface pressure of 30 mN m…”

mentioning

confidence: 98%

“…[26] Our monolayers are composed of POPG with one unsaturated chain. Therefore it might be possible that the higher surface-pressure increase observed here is partly due to the fact that a POPG monolayer is still in its liquid-expanded state at 30 mN m…”

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confidence: 99%

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Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

Erbe¹,

Kerth²,

Dathe³

et al. 2009

ChemBioChem

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Interactions of the cationic amphipathic peptide KLALKLALKALKAALKLA-NH(2) (KLAL) and its double D-amino acid replacement analogues l(11)k(12)-KLAL and k(9)a(10)-KLAL with lipid monolayers of anionic POPG, zwitterionic POPC and mixtures thereof at the air/water interface were investigated by infrared reflection- absorption spectroscopy (IRRAS). At high surface pressure (>30 mN m(-1)) all peptides incorporated into lipid monolayers containing at least 25 % anionic POPG, and adopted an alpha-helical conformation. Creation of free surface by expansion of the monolayers resulted in an additional adsorption of peptides from the subphase, but now in a beta-sheet conformation; this led to the coexistence of peptides in two distinctly different conformations within the lipid monolayer. The beta-sheets bound to the free surface could be squeezed out of the film by compressing the film to low surface areas, whereas the alpha-helices remained bound to the lipids until the film collapsed. When bound to the lipid monolayer, the helical axis of the peptides is oriented almost parallel to the surface of the monolayer.

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Section: Introductionmentioning

confidence: 99%

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confidence: 98%

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Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

Erbe¹,

Kerth²,

Dathe³

et al. 2009

ChemBioChem

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“…Investigations of the system using surface-sensitive IR spectroscopy (Fourier-transform infrared reflection adsorption spectroscopy, FT-IRRAS) will be reported in a forthcoming publication. 16 Specifically, the role of NPY's amphiphilic α-helix in the process of membrane binding is investigated by comparing native human NPY (hNPY) with a derivative, 17 Y20P−NPY, in which the 'helix breaker' proline replaces a tyrosine at position 20, in the center of the α-helix motif.…”

Section: Introductionmentioning

confidence: 99%

Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Film Balance and Fluorescence Microscopy Studies

Dyck

Lösche

2006

J. Phys. Chem. B

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The association of neuropeptide Y (NPY) with air/water interfaces and with phospholipid monolayers on water subphases and on physiological buffer has been investigated. Surface pressure (π) vs. molecular area (A) relations of the peptide at water surfaces depend on the concentration of the spreading solutions. Independent of that concentration, they show a transition from a low-density state to a high-density state at π ∼ 12 mN/m. Similar features are observed in the NPY adsorption to preformed monolayers (Δπ(t→∞) as a function of π i = π(t=0) where t = 0 signifies the time of peptide injection). The transition is also observed in cospread lipid/NPY monolayers and is interpreted as the exclusion of the peptide from the surface layer. The reproducibility of the isotherms after expansion suggests that cospread lipid/peptide monolayers are thermodynamically stable and that the peptide remains associated with the monolayer after exclusion from the lipid surface.A comparison of NPY association with zwitterionic and with anionic lipids, as well as a comparison of the interactions on pure water and on physiological buffer, suggests that electrostatic attraction plays a major role in the energetics of peptide binding to the membrane surface. Dual label fluorescence microscopy demonstrates that the peptide associates preferentially with the disordered liquid-condensed (LC) monolayer phase and also suggests that it self-aggregates upon exceeding a critical surface concentration. A NPY variant with a distorted α-helix interacts with the surface as strongly as the natural NPY but expands the monolayers more. This suggests that the helix motif in the peptide is more important for the interaction with the receptor than for binding of the peptide to the membrane surface. In context, these observations attribute a specific role to the membrane in funneling the signal peptide to its membrane receptor.

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“…These systems have significant advantages over bilayers, since they are stable systems, in which some parameters such as temperature, subphase composition (ie, pH and ionic strength) can be controlled with the advantage that monolayers of specific phospholipids like PE and CL can be formed, while they cannot be used above 20 mol% concentration to form a lipid vesicle [85]. Lipid monolayers have been extensively used to investigate the peptide-lipid interaction in the lipid-water interfaces [84,87,[150][151][152], providing information about the impact of peptide on the lipid packing [87].…”

Section: The Impact Of Peptides On the Lipid Packing Investigated By mentioning

confidence: 99%

Strategies for Exploring Electrostatic and Nonelectrostatic Contributions to the Interaction of Helical Antimicrobial Peptides with Model Membranes

Alvares

Cabrera

Neto

2016

Advances in Biomembranes and Lipid Self-Assembly

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Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Infrared Spectroscopic Characterization at the Air/Water Interface

Cited by 46 publications

References 33 publications

Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

Interactions of KLA Amphipathic Model Peptides with Lipid Monolayers

Interaction of the Neurotransmitter, Neuropeptide Y, with Phospholipid Membranes: Film Balance and Fluorescence Microscopy Studies

Strategies for Exploring Electrostatic and Nonelectrostatic Contributions to the Interaction of Helical Antimicrobial Peptides with Model Membranes

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