Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D. / Kielkopf, Claudia S; Whitten, Andrew E; Garner, Brett; Brown, Simon H J.

In: Bioscience Reports, Vol. 41, No. 1, 29.01.2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kielkopf, CS, Whitten, AE, Garner, B & Brown, SHJ 2021, 'Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D', Bioscience Reports, vol. 41, no. 1. https://doi.org/10.1042/BSR20201423

APA

Kielkopf, C. S., Whitten, A. E., Garner, B., & Brown, S. H. J. (2021). Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D. Bioscience Reports, 41(1). https://doi.org/10.1042/BSR20201423

Vancouver

Kielkopf CS, Whitten AE, Garner B, Brown SHJ. Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D. Bioscience Reports. 2021 Jan 29;41(1). https://doi.org/10.1042/BSR20201423

Author

Kielkopf, Claudia S ; Whitten, Andrew E ; Garner, Brett ; Brown, Simon H J. / Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D. In: Bioscience Reports. 2021 ; Vol. 41, No. 1.

Bibtex

@article{08a5cf4e737e45ce81de91c83eeda645,
title = "Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D",
abstract = "Human apolipoprotein-D (apoD) is a glycosylated lipocalin that plays a protective role in Alzheimer's disease due to its antioxidant function. Native apoD from human body fluids forms oligomers, predominantly a stable tetramer. As a lipocalin, apoD binds and transports small hydrophobic molecules such as progesterone, palmitic acid and sphingomyelin. Oligomerisation is a common trait in the lipocalin family and is affected by ligand binding in other lipocalins. The crystal structure of monomeric apoD shows no major changes upon progesterone binding. Here, we used small-angle X-ray scattering (SAXS) to investigate the influence of ligand binding and oxidation on apoD oligomerisation and conformation. As a solution-based technique, SAXS is well suited to detect changes in oligomeric state and conformation in response to ligand binding. Our results show no change in oligomeric state of apoD and no major conformational changes or subunit rearrangements in response to binding of ligands or protein oxidation. This highlights the highly stable structure of the native apoD tetramer under various physiologically relevant experimental conditions.",
author = "Kielkopf, {Claudia S} and Whitten, {Andrew E} and Brett Garner and Brown, {Simon H J}",
note = "{\textcopyright} 2021 The Author(s).",
year = "2021",
month = jan,
day = "29",
doi = "10.1042/BSR20201423",
language = "English",
volume = "41",
journal = "Bioscience Reports",
issn = "0144-8463",
publisher = "Portland Press Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Small angle X-ray scattering analysis of ligand-bound forms of tetrameric apolipoprotein-D

AU - Kielkopf, Claudia S

AU - Whitten, Andrew E

AU - Garner, Brett

AU - Brown, Simon H J

N1 - © 2021 The Author(s).

PY - 2021/1/29

Y1 - 2021/1/29

N2 - Human apolipoprotein-D (apoD) is a glycosylated lipocalin that plays a protective role in Alzheimer's disease due to its antioxidant function. Native apoD from human body fluids forms oligomers, predominantly a stable tetramer. As a lipocalin, apoD binds and transports small hydrophobic molecules such as progesterone, palmitic acid and sphingomyelin. Oligomerisation is a common trait in the lipocalin family and is affected by ligand binding in other lipocalins. The crystal structure of monomeric apoD shows no major changes upon progesterone binding. Here, we used small-angle X-ray scattering (SAXS) to investigate the influence of ligand binding and oxidation on apoD oligomerisation and conformation. As a solution-based technique, SAXS is well suited to detect changes in oligomeric state and conformation in response to ligand binding. Our results show no change in oligomeric state of apoD and no major conformational changes or subunit rearrangements in response to binding of ligands or protein oxidation. This highlights the highly stable structure of the native apoD tetramer under various physiologically relevant experimental conditions.

AB - Human apolipoprotein-D (apoD) is a glycosylated lipocalin that plays a protective role in Alzheimer's disease due to its antioxidant function. Native apoD from human body fluids forms oligomers, predominantly a stable tetramer. As a lipocalin, apoD binds and transports small hydrophobic molecules such as progesterone, palmitic acid and sphingomyelin. Oligomerisation is a common trait in the lipocalin family and is affected by ligand binding in other lipocalins. The crystal structure of monomeric apoD shows no major changes upon progesterone binding. Here, we used small-angle X-ray scattering (SAXS) to investigate the influence of ligand binding and oxidation on apoD oligomerisation and conformation. As a solution-based technique, SAXS is well suited to detect changes in oligomeric state and conformation in response to ligand binding. Our results show no change in oligomeric state of apoD and no major conformational changes or subunit rearrangements in response to binding of ligands or protein oxidation. This highlights the highly stable structure of the native apoD tetramer under various physiologically relevant experimental conditions.

U2 - 10.1042/BSR20201423

DO - 10.1042/BSR20201423

M3 - Journal article

C2 - 33399852

VL - 41

JO - Bioscience Reports

JF - Bioscience Reports

SN - 0144-8463

IS - 1

ER -

ID: 285315101