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

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  • Jitka Petrlova
    Department of Experimental Medical Science Lund University BMC Floor C12 SE‐221 84 Lund Sweden
  • Arnab Bhattacherjee
    Computational Biology and Biological Physics, Department of Astronomy and Theoretical Physics Lund University Sölvegatan 14A SE‐223 62 Lund Sweden
  • Wouter Boomsma
    Computational Biology and Biological Physics, Department of Astronomy and Theoretical Physics Lund University Sölvegatan 14A SE‐223 62 Lund Sweden
  • Stefan Wallin
    Computational Biology and Biological Physics, Department of Astronomy and Theoretical Physics Lund University Sölvegatan 14A SE‐223 62 Lund Sweden
  • Jens O. Lagerstedt
    Department of Experimental Medical Science Lund University BMC Floor C12 SE‐221 84 Lund Sweden
  • Anders Irbäck
    Computational Biology and Biological Physics, Department of Astronomy and Theoretical Physics Lund University Sölvegatan 14A SE‐223 62 Lund Sweden

書誌事項

公開日
2014-08-23
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1002/pro.2534
公開者
Wiley

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説明

<jats:title>Abstract</jats:title><jats:p>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.</jats:p>

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