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Jens Lagerstedt

Associate professor

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Synchrotron radiation circular dichroism spectroscopy reveals structural divergences in HDL-bound apoA-I variants

Author

  • Rita Del Giudice
  • Oktawia Nilsson
  • Joan Domingo-Espín
  • Jens O Lagerstedt

Summary, in English

Apolipoprotein A-I (apoA-I) in high-density lipoprotein (HDL) provides cardiovascular protection. Synchrotron radiation circular dichroism (SRCD) spectroscopy was used to analyze the dynamic solution structure of the apoA-I protein in the apo- and HDL-states and the protein structure conversion in HDL formation. Wild-type apoA-I protein was compared to human variants that either are protective (R173C, Milano) or lead to increased risk for ischaemic heart disease (A164S). Comparable secondary structure distributions in the HDL particles, including significant levels of beta strand/turn, were observed. ApoA-I Milano in HDL displayed larger size heterogeneity, increased protein flexibility, and an altered lipid-binding profile, whereas the apoA-I A164S in HDL showed decrease thermal stability, potentially linking the intrinsic HDL propensities of the variants to disease risk.

Department/s

  • Medical Protein Science
  • EXODIAB: Excellence in Diabetes Research in Sweden

Publishing year

2017-10-19

Language

English

Publication/Series

Scientific Reports

Volume

7

Issue

1

Document type

Journal article

Publisher

Nature Publishing Group

Topic

  • Medical Biotechnology

Status

Published

Research group

  • Medical Protein Science

ISBN/ISSN/Other

  • ISSN: 2045-2322