The N-terminal segment of pulmonary surfactant lipopeptide SP-C has intrinsic propensity to interact with and perturb phospholipid bilayers.

Inés Plasencia, Luis Rivas, Kevin M W Keough, Derek Marsh, Jesús Pérez-Gil

Research output: Contribution to journalJournal articleResearch

Abstract

In the present study, 13-residue peptides with sequences corresponding to the native N-terminal segment of pulmonary SP-C (surfactant protein C) have been synthesized and their interaction with phospholipid bilayers characterized. The peptides are soluble in aqueous media but associate spontaneously with bilayers composed of either zwitterionic (phosphatidylcholine) or anionic (phosphatidylglycerol) phospholipids. The peptides show higher affinity for anionic than for zwitterionic membranes. Interaction of the peptides with both zwitterionic and anionic membranes promotes phospholipid vesicle aggregation, and leakage of the aqueous content of the vesicles. The lipid-peptide interaction includes a significant hydrophobic component for both zwitterionic and anionic membranes, although the interaction with phosphatidylglycerol bilayers is also electrostatic in nature. The effects of the SP-C N-terminal peptides on the membrane structure are mediated by significant perturbations of the packing order and mobility of phospholipid acyl chain segments deep in the bilayer, as detected by differential scanning calorimetry and spin-label ESR. These results suggest that the N-terminal region of SP-C, even in the absence of acylation, possesses an intrinsic propensity to interact with and perturb phospholipid bilayers, thereby potentially facilitating SP-C promoting bilayer-monolayer transitions at the alveolar spaces.
Udgivelsesdato: 2004-Jan-1
Original languageEnglish
JournalBiochemical Journal
Volume377
Issue numberPt 1
Pages (from-to)183-193
Number of pages10
ISSN0264-6021
DOIs
Publication statusPublished - 1. Jan 2004

Keywords

  • Amino Acid Sequence
  • Binding Sites
  • Calorimetry, Differential Scanning
  • Electron Spin Resonance Spectroscopy
  • Lipid Bilayers
  • Peptides
  • Phospholipids
  • Pulmonary Surfactant-Associated Protein C
  • Spectrometry, Fluorescence
  • Tryptophan

Cite this

Plasencia, Inés ; Rivas, Luis ; Keough, Kevin M W ; Marsh, Derek ; Pérez-Gil, Jesús. / The N-terminal segment of pulmonary surfactant lipopeptide SP-C has intrinsic propensity to interact with and perturb phospholipid bilayers. In: Biochemical Journal. 2004 ; Vol. 377, No. Pt 1. pp. 183-193.
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abstract = "In the present study, 13-residue peptides with sequences corresponding to the native N-terminal segment of pulmonary SP-C (surfactant protein C) have been synthesized and their interaction with phospholipid bilayers characterized. The peptides are soluble in aqueous media but associate spontaneously with bilayers composed of either zwitterionic (phosphatidylcholine) or anionic (phosphatidylglycerol) phospholipids. The peptides show higher affinity for anionic than for zwitterionic membranes. Interaction of the peptides with both zwitterionic and anionic membranes promotes phospholipid vesicle aggregation, and leakage of the aqueous content of the vesicles. The lipid-peptide interaction includes a significant hydrophobic component for both zwitterionic and anionic membranes, although the interaction with phosphatidylglycerol bilayers is also electrostatic in nature. The effects of the SP-C N-terminal peptides on the membrane structure are mediated by significant perturbations of the packing order and mobility of phospholipid acyl chain segments deep in the bilayer, as detected by differential scanning calorimetry and spin-label ESR. These results suggest that the N-terminal region of SP-C, even in the absence of acylation, possesses an intrinsic propensity to interact with and perturb phospholipid bilayers, thereby potentially facilitating SP-C promoting bilayer-monolayer transitions at the alveolar spaces. Udgivelsesdato: 2004-Jan-1",
keywords = "Amino Acid Sequence, Binding Sites, Calorimetry, Differential Scanning, Electron Spin Resonance Spectroscopy, Lipid Bilayers, Peptides, Phospholipids, Pulmonary Surfactant-Associated Protein C, Spectrometry, Fluorescence, Tryptophan",
author = "In{\'e}s Plasencia and Luis Rivas and Keough, {Kevin M W} and Derek Marsh and Jes{\'u}s P{\'e}rez-Gil",
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The N-terminal segment of pulmonary surfactant lipopeptide SP-C has intrinsic propensity to interact with and perturb phospholipid bilayers. / Plasencia, Inés; Rivas, Luis; Keough, Kevin M W; Marsh, Derek; Pérez-Gil, Jesús.

In: Biochemical Journal, Vol. 377, No. Pt 1, 01.01.2004, p. 183-193.

Research output: Contribution to journalJournal articleResearch

TY - JOUR

T1 - The N-terminal segment of pulmonary surfactant lipopeptide SP-C has intrinsic propensity to interact with and perturb phospholipid bilayers.

AU - Plasencia, Inés

AU - Rivas, Luis

AU - Keough, Kevin M W

AU - Marsh, Derek

AU - Pérez-Gil, Jesús

PY - 2004/1/1

Y1 - 2004/1/1

N2 - In the present study, 13-residue peptides with sequences corresponding to the native N-terminal segment of pulmonary SP-C (surfactant protein C) have been synthesized and their interaction with phospholipid bilayers characterized. The peptides are soluble in aqueous media but associate spontaneously with bilayers composed of either zwitterionic (phosphatidylcholine) or anionic (phosphatidylglycerol) phospholipids. The peptides show higher affinity for anionic than for zwitterionic membranes. Interaction of the peptides with both zwitterionic and anionic membranes promotes phospholipid vesicle aggregation, and leakage of the aqueous content of the vesicles. The lipid-peptide interaction includes a significant hydrophobic component for both zwitterionic and anionic membranes, although the interaction with phosphatidylglycerol bilayers is also electrostatic in nature. The effects of the SP-C N-terminal peptides on the membrane structure are mediated by significant perturbations of the packing order and mobility of phospholipid acyl chain segments deep in the bilayer, as detected by differential scanning calorimetry and spin-label ESR. These results suggest that the N-terminal region of SP-C, even in the absence of acylation, possesses an intrinsic propensity to interact with and perturb phospholipid bilayers, thereby potentially facilitating SP-C promoting bilayer-monolayer transitions at the alveolar spaces. Udgivelsesdato: 2004-Jan-1

AB - In the present study, 13-residue peptides with sequences corresponding to the native N-terminal segment of pulmonary SP-C (surfactant protein C) have been synthesized and their interaction with phospholipid bilayers characterized. The peptides are soluble in aqueous media but associate spontaneously with bilayers composed of either zwitterionic (phosphatidylcholine) or anionic (phosphatidylglycerol) phospholipids. The peptides show higher affinity for anionic than for zwitterionic membranes. Interaction of the peptides with both zwitterionic and anionic membranes promotes phospholipid vesicle aggregation, and leakage of the aqueous content of the vesicles. The lipid-peptide interaction includes a significant hydrophobic component for both zwitterionic and anionic membranes, although the interaction with phosphatidylglycerol bilayers is also electrostatic in nature. The effects of the SP-C N-terminal peptides on the membrane structure are mediated by significant perturbations of the packing order and mobility of phospholipid acyl chain segments deep in the bilayer, as detected by differential scanning calorimetry and spin-label ESR. These results suggest that the N-terminal region of SP-C, even in the absence of acylation, possesses an intrinsic propensity to interact with and perturb phospholipid bilayers, thereby potentially facilitating SP-C promoting bilayer-monolayer transitions at the alveolar spaces. Udgivelsesdato: 2004-Jan-1

KW - Amino Acid Sequence

KW - Binding Sites

KW - Calorimetry, Differential Scanning

KW - Electron Spin Resonance Spectroscopy

KW - Lipid Bilayers

KW - Peptides

KW - Phospholipids

KW - Pulmonary Surfactant-Associated Protein C

KW - Spectrometry, Fluorescence

KW - Tryptophan

U2 - 10.1042/BJ20030815

DO - 10.1042/BJ20030815

M3 - Journal article

VL - 377

SP - 183

EP - 193

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - Pt 1

ER -