Synchrotron radiation circular dichroism spectroscopy reveals structural divergences in HDL-bound apoA-I variants
| Autor: | Oktawia Nilsson, Joan Domingo-Espín, Jens O. Lagerstedt, Rita Del Giudice |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Apolipoprotein B Beta sheet lcsh:Medicine Polymorphism Single Nucleotide Article Turn (biochemistry) 03 medical and health sciences Protein structure Humans Transition Temperature lcsh:Science Spectroscopy Protein secondary structure Multidisciplinary 030102 biochemistry & molecular biology biology Apolipoprotein A-I Chemistry Protein Stability Circular Dichroism lcsh:R nutritional and metabolic diseases Synchrotron radiation circular dichroism 030104 developmental biology Biophysics biology.protein lcsh:Q lipids (amino acids peptides and proteins) Protein Conformation beta-Strand Lipoproteins HDL Synchrotrons Lipoprotein Protein Binding |
| Zdroj: | Scientific Reports Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017) |
| ISSN: | 2045-2322 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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