Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment

Valeriya M. Trusova; Galyna P. Gorbenko; Pabak Sarkar; Rafal Luchowski; Irina Akopova; Leonid D. Patsenker; Oleksii Klochko; Anatoliy L. Tatarets; Yuliia O. Kudriavtseva; Ewald A. Terpetschnig; Ignacy Gryczynski; Zygmunt Gryczynski

doi:10.1021/jp108976e

Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment

Valeriya M. Trusova, Galyna P. Gorbenko, Pabak Sarkar, Rafal Luchowski, Irina Akopova, Leonid D. Patsenker, Oleksii Klochko, Anatoliy L. Tatarets, Yuliia O. Kudriavtseva, Ewald A. Terpetschnig, Ignacy Gryczynski, Zygmunt Gryczynski

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

6 Scopus citations

Abstract

Intermolecular time-resolved and single-molecule Förster resonance energy transfer (FRET) have been applied to detect quantitatively the aggregation of polycationic protein lysozyme (Lz) in the presence of lipid vesicles composed of phosphatidylcholine (PC) and its mixture with 5, 10, 20, or 40 mol % of phosphatidylglycerol (PG) (PG5, PG10, PG20, or PG40, respectively). Upon binding to PC, PG5, or PG10 model membranes, Lz was found to retain its native monomeric conformation, while increasing content of anionic lipid up to 20 or 40 mol % resulted in the formation of Lz aggregates. The structural parameters of protein self-association (the degree of oligomerization, the distance between the monomers in protein assembly, and the fraction of donors present in oligomers) have been derived. The crucial role of the factors such as lateral density of the adsorbed protein and electrostatic and hydrophobic Lz-lipid interactions in controlling the protein self-association behavior has been proposed.

Original language	English
Pages (from-to)	16773-16782
Number of pages	10
Journal	Journal of Physical Chemistry B
Volume	114
Issue number	50
DOIs	https://doi.org/10.1021/jp108976e
State	Published - 23 Dec 2010
Externally published	Yes

Access to Document

10.1021/jp108976e

Cite this

Trusova, V. M., Gorbenko, G. P., Sarkar, P., Luchowski, R., Akopova, I., Patsenker, L. D., Klochko, O., Tatarets, A. L., Kudriavtseva, Y. O., Terpetschnig, E. A., Gryczynski, I., & Gryczynski, Z. (2010). Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment. Journal of Physical Chemistry B, 114(50), 16773-16782. https://doi.org/10.1021/jp108976e

@article{a41bde1c50da4f989d9d66e4a28868c8,

title = "F{\"o}rster resonance energy transfer evidence for lysozyme oligomerization in lipid environment",

abstract = "Intermolecular time-resolved and single-molecule F{\"o}rster resonance energy transfer (FRET) have been applied to detect quantitatively the aggregation of polycationic protein lysozyme (Lz) in the presence of lipid vesicles composed of phosphatidylcholine (PC) and its mixture with 5, 10, 20, or 40 mol % of phosphatidylglycerol (PG) (PG5, PG10, PG20, or PG40, respectively). Upon binding to PC, PG5, or PG10 model membranes, Lz was found to retain its native monomeric conformation, while increasing content of anionic lipid up to 20 or 40 mol % resulted in the formation of Lz aggregates. The structural parameters of protein self-association (the degree of oligomerization, the distance between the monomers in protein assembly, and the fraction of donors present in oligomers) have been derived. The crucial role of the factors such as lateral density of the adsorbed protein and electrostatic and hydrophobic Lz-lipid interactions in controlling the protein self-association behavior has been proposed.",

author = "Trusova, {Valeriya M.} and Gorbenko, {Galyna P.} and Pabak Sarkar and Rafal Luchowski and Irina Akopova and Patsenker, {Leonid D.} and Oleksii Klochko and Tatarets, {Anatoliy L.} and Kudriavtseva, {Yuliia O.} and Terpetschnig, {Ewald A.} and Ignacy Gryczynski and Zygmunt Gryczynski",

year = "2010",

month = dec,

day = "23",

doi = "10.1021/jp108976e",

language = "אנגלית",

volume = "114",

pages = "16773--16782",

journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

publisher = "American Chemical Society",

number = "50",

}

Trusova, VM, Gorbenko, GP, Sarkar, P, Luchowski, R, Akopova, I, Patsenker, LD, Klochko, O, Tatarets, AL, Kudriavtseva, YO, Terpetschnig, EA, Gryczynski, I & Gryczynski, Z 2010, 'Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment', Journal of Physical Chemistry B, vol. 114, no. 50, pp. 16773-16782. https://doi.org/10.1021/jp108976e

TY - JOUR

T1 - Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment

AU - Trusova, Valeriya M.

AU - Gorbenko, Galyna P.

AU - Sarkar, Pabak

AU - Luchowski, Rafal

AU - Akopova, Irina

AU - Patsenker, Leonid D.

AU - Klochko, Oleksii

AU - Tatarets, Anatoliy L.

AU - Kudriavtseva, Yuliia O.

AU - Terpetschnig, Ewald A.

AU - Gryczynski, Ignacy

AU - Gryczynski, Zygmunt

PY - 2010/12/23

Y1 - 2010/12/23

N2 - Intermolecular time-resolved and single-molecule Förster resonance energy transfer (FRET) have been applied to detect quantitatively the aggregation of polycationic protein lysozyme (Lz) in the presence of lipid vesicles composed of phosphatidylcholine (PC) and its mixture with 5, 10, 20, or 40 mol % of phosphatidylglycerol (PG) (PG5, PG10, PG20, or PG40, respectively). Upon binding to PC, PG5, or PG10 model membranes, Lz was found to retain its native monomeric conformation, while increasing content of anionic lipid up to 20 or 40 mol % resulted in the formation of Lz aggregates. The structural parameters of protein self-association (the degree of oligomerization, the distance between the monomers in protein assembly, and the fraction of donors present in oligomers) have been derived. The crucial role of the factors such as lateral density of the adsorbed protein and electrostatic and hydrophobic Lz-lipid interactions in controlling the protein self-association behavior has been proposed.

AB - Intermolecular time-resolved and single-molecule Förster resonance energy transfer (FRET) have been applied to detect quantitatively the aggregation of polycationic protein lysozyme (Lz) in the presence of lipid vesicles composed of phosphatidylcholine (PC) and its mixture with 5, 10, 20, or 40 mol % of phosphatidylglycerol (PG) (PG5, PG10, PG20, or PG40, respectively). Upon binding to PC, PG5, or PG10 model membranes, Lz was found to retain its native monomeric conformation, while increasing content of anionic lipid up to 20 or 40 mol % resulted in the formation of Lz aggregates. The structural parameters of protein self-association (the degree of oligomerization, the distance between the monomers in protein assembly, and the fraction of donors present in oligomers) have been derived. The crucial role of the factors such as lateral density of the adsorbed protein and electrostatic and hydrophobic Lz-lipid interactions in controlling the protein self-association behavior has been proposed.

UR - http://www.scopus.com/inward/record.url?scp=78650320093&partnerID=8YFLogxK

U2 - 10.1021/jp108976e

DO - 10.1021/jp108976e

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:78650320093

SN - 1520-6106

VL - 114

SP - 16773

EP - 16782

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 50

ER -

Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment

Abstract

Access to Document

Other files and links

Fingerprint

Cite this