Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC

Antje Pokorny; Lindsay E. Yandek; Adekunle I. Elegbede; Anne Hinderliter; Paulo F.F. Almeida

doi:10.1529/biophysj.106.085027

Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC

Antje Pokorny
, Lindsay E. Yandek
, Adekunle I. Elegbede
, Anne Hinderliter
, Paulo F.F. Almeida

Chemistry & Biochemistry

Research output: Contribution to journal › Article › peer-review

90 Scopus citations

Abstract

The kinetics of carboxyfluorescein efflux induced by the amphipathic peptide δ-lysin from vesicles of porcine brain sphingomyelin (BSM), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and cholesterol (Chol) were investigated as a function of temperature and composition. Sphingomyelin (SM)/Chol mixtures form a liquid-ordered (L_o) phase whereas POPC exists in the liquid-disordered (L_d) phase at ambient temperature. δ-Lysin binds strongly to L_d and poorly to L_o phase. In BSM/Chol/POPC vesicles the rate of carboxyfluorescein efflux induced by δ-lysin increases as the POPC content decreases. This is explained by the increase of δ-lysin concentration in L_d domains, which enhances membrane perturbation by the peptide. Phase separations in the micrometer scale have been observed by fluorescence microscopy in SM/Chol/POPC mixtures for some SM, though not for BSM. Thus, δ-lysin must detect heterogeneities (domains) in BSM/Chol/POPC on a much smaller scale. Advantage was taken of the inverse variation of the efflux rate with the L_d content of BSM/Chol/POPC vesicles to estimate the L_d fraction in those mixtures. These results were combined with differential scanning calorimetry to obtain the BSM/Chol/POPC phase diagram as a function of temperature.

Original language	English (US)
Pages (from-to)	2184-2197
Number of pages	14
Journal	Biophysical journal
Volume	91
Issue number	6
DOIs	https://doi.org/10.1529/biophysj.106.085027
State	Published - 2006

Bibliographical note

Funding Information:
This work was supported in part by National Institutes of Health grants No. GM072507 (University of North Carolina Wilmington) and No. GM064443 (North Dakota State University).

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10.1529/biophysj.106.085027

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title = "Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC",

abstract = "The kinetics of carboxyfluorescein efflux induced by the amphipathic peptide δ-lysin from vesicles of porcine brain sphingomyelin (BSM), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and cholesterol (Chol) were investigated as a function of temperature and composition. Sphingomyelin (SM)/Chol mixtures form a liquid-ordered (Lo) phase whereas POPC exists in the liquid-disordered (Ld) phase at ambient temperature. δ-Lysin binds strongly to Ld and poorly to Lo phase. In BSM/Chol/POPC vesicles the rate of carboxyfluorescein efflux induced by δ-lysin increases as the POPC content decreases. This is explained by the increase of δ-lysin concentration in Ld domains, which enhances membrane perturbation by the peptide. Phase separations in the micrometer scale have been observed by fluorescence microscopy in SM/Chol/POPC mixtures for some SM, though not for BSM. Thus, δ-lysin must detect heterogeneities (domains) in BSM/Chol/POPC on a much smaller scale. Advantage was taken of the inverse variation of the efflux rate with the Ld content of BSM/Chol/POPC vesicles to estimate the Ld fraction in those mixtures. These results were combined with differential scanning calorimetry to obtain the BSM/Chol/POPC phase diagram as a function of temperature.",

author = "Antje Pokorny and Yandek, \{Lindsay E.\} and Elegbede, \{Adekunle I.\} and Anne Hinderliter and Almeida, \{Paulo F.F.\}",

note = "Funding Information: This work was supported in part by National Institutes of Health grants No. GM072507 (University of North Carolina Wilmington) and No. GM064443 (North Dakota State University). ",

year = "2006",

doi = "10.1529/biophysj.106.085027",

language = "English (US)",

volume = "91",

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T1 - Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC

AU - Pokorny, Antje

AU - Yandek, Lindsay E.

AU - Elegbede, Adekunle I.

AU - Hinderliter, Anne

AU - Almeida, Paulo F.F.

N1 - Funding Information: This work was supported in part by National Institutes of Health grants No. GM072507 (University of North Carolina Wilmington) and No. GM064443 (North Dakota State University).

PY - 2006

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N2 - The kinetics of carboxyfluorescein efflux induced by the amphipathic peptide δ-lysin from vesicles of porcine brain sphingomyelin (BSM), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and cholesterol (Chol) were investigated as a function of temperature and composition. Sphingomyelin (SM)/Chol mixtures form a liquid-ordered (Lo) phase whereas POPC exists in the liquid-disordered (Ld) phase at ambient temperature. δ-Lysin binds strongly to Ld and poorly to Lo phase. In BSM/Chol/POPC vesicles the rate of carboxyfluorescein efflux induced by δ-lysin increases as the POPC content decreases. This is explained by the increase of δ-lysin concentration in Ld domains, which enhances membrane perturbation by the peptide. Phase separations in the micrometer scale have been observed by fluorescence microscopy in SM/Chol/POPC mixtures for some SM, though not for BSM. Thus, δ-lysin must detect heterogeneities (domains) in BSM/Chol/POPC on a much smaller scale. Advantage was taken of the inverse variation of the efflux rate with the Ld content of BSM/Chol/POPC vesicles to estimate the Ld fraction in those mixtures. These results were combined with differential scanning calorimetry to obtain the BSM/Chol/POPC phase diagram as a function of temperature.

AB - The kinetics of carboxyfluorescein efflux induced by the amphipathic peptide δ-lysin from vesicles of porcine brain sphingomyelin (BSM), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and cholesterol (Chol) were investigated as a function of temperature and composition. Sphingomyelin (SM)/Chol mixtures form a liquid-ordered (Lo) phase whereas POPC exists in the liquid-disordered (Ld) phase at ambient temperature. δ-Lysin binds strongly to Ld and poorly to Lo phase. In BSM/Chol/POPC vesicles the rate of carboxyfluorescein efflux induced by δ-lysin increases as the POPC content decreases. This is explained by the increase of δ-lysin concentration in Ld domains, which enhances membrane perturbation by the peptide. Phase separations in the micrometer scale have been observed by fluorescence microscopy in SM/Chol/POPC mixtures for some SM, though not for BSM. Thus, δ-lysin must detect heterogeneities (domains) in BSM/Chol/POPC on a much smaller scale. Advantage was taken of the inverse variation of the efflux rate with the Ld content of BSM/Chol/POPC vesicles to estimate the Ld fraction in those mixtures. These results were combined with differential scanning calorimetry to obtain the BSM/Chol/POPC phase diagram as a function of temperature.

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ER -

Temperature and composition dependence of the interaction of δ-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC

Abstract

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