Lipid - Peptide communication in fluid bilayers

Journal of the American Chemical Society

Volumn 120, Issue 15, 1998, Pages 3758-3761

  Shibakami, Motonari ^a   Inagaki, Minoru ^a   Regen, Steven L ^a  

^a LEHIGH UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DIPALMITOYLPHOSPHATIDYLCHOLINE; DISULFIDE; GRAMICIDIN A; MONOMER; MYRISTIC ACID; PEPTIDE; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID; STEARIC ACID;

ARTICLE; BILAYER MEMBRANE; CHANNEL GATING; HYDROPHOBICITY; LIQUID MEMBRANE; MOLECULAR RECOGNITION; PHOSPHOLIPID MEMBRANE; PHOSPHOLIPID VESICLE; PROTEIN CONFORMATION; PROTEIN LIPID INTERACTION; SIGNAL TRANSDUCTION;

EID: 0032557196     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9737275     Document Type: Article

References (22)

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8. 15-ethanolamine. The peptide was purchased from Fluka (≥90%) and used directly.
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13. CD spectra were obtained on an AVIV 62ADS CD spectrometer that was equipped with computer-controlled data acquisition and analysis. The path length was 1 mm, and vesicles without gA were taken as the baseline.
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15. The equilibrium dimer ratio was derived from experiments with heterodimer-based vesicles.
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18. Vesicles were also examined by optical microscopy on an Olympus DC-70 microscope in bright field or Normarski DIC configurations, equipped with a 100 x UplanApo (NA = 1.35) oil imersion objective. In the absence of peptide, spherical particles were readily apparent having a mean diameter of 1.26 ± 0.36 μm. In the presence of 2% c-gA or 2% nc-gA, spherical particles were observed having mean diameters of 0.93 ± 0.24 and 0.98 ± 0.39 μm, respectively. Mean diameters and standard deviations were determined by measuring at least 90 vesicles.
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20. + calcd 736.4587, found 736.4585.
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22. 8-10 (22) An interesting alternate model (proposed by a Reviewer) is that the longer phospholipid may preferentially orient around nc-gA with the chain ends filling in any voids around the end of the peptide.