Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I

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Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I. / Petrlova, Jitka; Bhattacherjee, Arnab; Boomsma, Wouter Krogh; Wallin, Stefan; Lagerstedt, Jens O.; Irbäck, Anders.

In: Protein Science, Vol. 23, No. 11, 2014, p. 1559-1571.

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

Harvard

Petrlova, J, Bhattacherjee, A, Boomsma, WK, Wallin, S, Lagerstedt, JO & Irbäck, A 2014, 'Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I', Protein Science, vol. 23, no. 11, pp. 1559-1571. https://doi.org/10.1002/pro.2534

APA

Petrlova, J., Bhattacherjee, A., Boomsma, W. K., Wallin, S., Lagerstedt, J. O., & Irbäck, A. (2014). Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I. Protein Science, 23(11), 1559-1571. https://doi.org/10.1002/pro.2534

Vancouver

Petrlova J, Bhattacherjee A, Boomsma WK, Wallin S, Lagerstedt JO, Irbäck A. Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I. Protein Science. 2014;23(11):1559-1571. https://doi.org/10.1002/pro.2534

Author

Petrlova, Jitka ; Bhattacherjee, Arnab ; Boomsma, Wouter Krogh ; Wallin, Stefan ; Lagerstedt, Jens O. ; Irbäck, Anders. / Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I. In: Protein Science. 2014 ; Vol. 23, No. 11. pp. 1559-1571.

Bibtex

@article{9f623d47d2e24370a7ceba440e5bd470,

title = "Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I",

abstract = "Several disease-linked mutations of apolipoprotein A-I, the major protein in high-density lipoprotein (HDL), are known to be amyloidogenic, and the fibrils often contain N-terminal fragments of the protein. Here, we present a combined computational and experimental study of the fibril-associated disordered 1-93 fragment of this protein, in wild-type and mutated (G26R, S36A, K40L, W50R) forms. In atomic-level Monte Carlo simulations of the free monomer, validated by circular dichroism spectroscopy, we observe changes in the position-dependent β-strand probability induced by mutations. We find that these conformational shifts match well with the effects of these mutations in thioflavin T fluorescence and transmission electron microscopy experiments. Together, our results point to molecular mechanisms that may have a key role in disease-linked aggregation of apolipoprotein A-I.",

author = "Jitka Petrlova and Arnab Bhattacherjee and Boomsma, {Wouter Krogh} and Stefan Wallin and Lagerstedt, {Jens O.} and Anders Irb{\"a}ck",

note = "{\textcopyright} 2014 The Protein Society.",

year = "2014",

doi = "10.1002/pro.2534",

language = "English",

volume = "23",

pages = "1559--1571",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Wiley-Blackwell",

number = "11",

}

RIS

TY - JOUR

T1 - Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I

AU - Petrlova, Jitka

AU - Bhattacherjee, Arnab

AU - Boomsma, Wouter Krogh

AU - Wallin, Stefan

AU - Lagerstedt, Jens O.

AU - Irbäck, Anders

PY - 2014

Y1 - 2014

N2 - Several disease-linked mutations of apolipoprotein A-I, the major protein in high-density lipoprotein (HDL), are known to be amyloidogenic, and the fibrils often contain N-terminal fragments of the protein. Here, we present a combined computational and experimental study of the fibril-associated disordered 1-93 fragment of this protein, in wild-type and mutated (G26R, S36A, K40L, W50R) forms. In atomic-level Monte Carlo simulations of the free monomer, validated by circular dichroism spectroscopy, we observe changes in the position-dependent β-strand probability induced by mutations. We find that these conformational shifts match well with the effects of these mutations in thioflavin T fluorescence and transmission electron microscopy experiments. Together, our results point to molecular mechanisms that may have a key role in disease-linked aggregation of apolipoprotein A-I.

AB - Several disease-linked mutations of apolipoprotein A-I, the major protein in high-density lipoprotein (HDL), are known to be amyloidogenic, and the fibrils often contain N-terminal fragments of the protein. Here, we present a combined computational and experimental study of the fibril-associated disordered 1-93 fragment of this protein, in wild-type and mutated (G26R, S36A, K40L, W50R) forms. In atomic-level Monte Carlo simulations of the free monomer, validated by circular dichroism spectroscopy, we observe changes in the position-dependent β-strand probability induced by mutations. We find that these conformational shifts match well with the effects of these mutations in thioflavin T fluorescence and transmission electron microscopy experiments. Together, our results point to molecular mechanisms that may have a key role in disease-linked aggregation of apolipoprotein A-I.

U2 - 10.1002/pro.2534

DO - 10.1002/pro.2534

M3 - Journal article

C2 - 25131953

VL - 23

SP - 1559

EP - 1571

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 11

ER -

ID: 123508160

Forskning