Calorimetric and fourier transform infrared spectroscopic studies on the interaction of glycophorin with phosphatidylserine/dipalmitoylphosphatidylcholine-d62 mixtures

Download
  1. Get@NRC: Calorimetric and fourier transform infrared spectroscopic studies on the interaction of glycophorin with phosphatidylserine/dipalmitoylphosphatidylcholine-d62 mixtures (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1016/0005-2736(84)90297-9
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleBiochimica et Biophysica Acta (BBA) - Biomembranes
ISSN0005-2736
Volume774
Issue2
Pages237246
SubjectLipid-protein interaction; Phase transition; Infrared spectroscopy; Calorimetry; Glycophorin; Phospholipid vesicle
AbstractGlycophorin has been isolated in pure form from human erythrocyte membranes and reconstituted into lipid vesicles composed of binary mixtures of bovine brain phosphatidylserine (PS) and acyl-chain perdeuterated dipalmitoyiphosphatidylcholine (DPPC-d₆₂). The effect of protein on lipid melting behavior and order has been monitored with differential scanning calorimetry and Fourier transform infrared spectroscopy (FT-IR). The phase diagram for PS/DPPC-d₆₂ is consistent with that previously reported for PS/DPPC (Stewart et al. (1979) Biochim. Biophys. Acta 556, 1-16) and indicates that acyl chain perdeuteration does not greatly alter the lipid mixing characteristics. The use of deuterated lipid allows the examination of lipid order by FT-IR of each lipid component in the binary mixtures as well as in the ternary (lipid/lipid/protein) systems. Addition of glycophorin to a 30:70 PS/DPPC-d₆₂ binary lipid mixture results in a preferential glycophorin/PS interaction leading to bulk lipid enriched in DPPC-d₆₂. This is revealed in two ways: first, through cooperative calorimetric transitions increased in temperature from the binary lipid system and second, through FT-IR melting curves of the DPPC-d₆₂ component which shows transitions increased in both onset and completion temperatures in the presence of protein. In addition, non-cooperative melting events are observed at temperatures below the onset of phase separation. The FT-IR data are used to assign these non-cooperative events to the melting of the PS component. For the 50:50 lipid mixture with protein, two transitions are observed in the DSC experiments. The IR results indicate that both lipid components are involved with the lower temperature event.
Publication date
PublisherElsevier B.V.
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001264
Export citationExport as RIS
Report a correctionReport a correction
Record identifier082bd141-a58e-4d8c-b725-37b4d8b7503d
Record created2017-01-12
Record modified2017-01-12
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)