The structure of human apolipoprotein E2, E3 and E4 in solution. 2. Multidomain organization correlates with the stability of apoE structure
Abstract
The stabilities toward thermal and chemical denaturation of three recombinant isoforms of human apolipoprotein E (r-apoE2, r-apoE3 and r-apoE4), human plasma apoE3, the recombinant amino-terminal (NT) and the carboxyl-terminal (CT) domains of plasma apoE3 at pH 7 were studied using near and far ultraviolet circular dichroism (UV CD), fluorescence and size-exclusion chromatography. By far UV CD, thermal unfolding was irreversible for the intact apoE isoforms and consisted of a single transition. The r-apoE3 was found to be less stable as compared to the plasma protein and the stability of recombinant isoforms was r-apoE4<r-apoE3<r-apoE2. The thermal denaturation of the isolated NT- and CT-domains of apoE3 was largely reversible and included two transitions. The NT-domain was more resistant to heating than the CT-domain, both of which were more resistant than the intact protein. By near UV CD, the thermal unfolding was biphasic. When compared, thermal unfolding of the secondary and tertiary structures appeared to occur concurrently in r-apoE2 whereas heating affected the tertiary structure, initially, in r-apoE3 and r-apoE4. Denaturation with guanidine hydrochloride did not follow a two-state transition. A three-state treatment of the denaturation curves revealed the order of stability as r-apoE4<r-apoE3<r-apoE2 for the whole proteins as well as that for the NT-domains, as established by fluorescence and far UV CD spectroscopy, whereas the CT-domains had roughly similar stabili…
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ApoE is prone to aggregation and forms oligomeric structures in solution.
“Furthermore, apoE has been shown to be prone to aggregation and to form oligomeric structures in solution (21,22).”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [35]
Thermal denaturation analysis was used as a method of comparing changes between apoE3 variants despite the process being gradual multistate and not fully reversible, because irreversible changes are relatively slow compared with heat unfolding.
“Although the thermal denaturation of apoE3 is a gradual multistate and not fully reversible process, such analysis has been used before as a method of comparing changes between apoE3 variants, primarily because the irreversible changes are relatively slow compared with the heat unfolding (34,35).”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [35]
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- Authors
- Clément-Collin, V., Barbier, A., Dergunov, A. D., Visvikis, A., Siest, G., Desmadril, M., Takahashi, M., & Aggerbeck, L. P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- National Research Center for Preventive Medicine (RU)
- Université Henri Poincaré (FR)
- Université Paris-Sud (FR)
- Corresponding author
- Dergunov, Alexander D.
- Venue
- Biophysical Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-01
- Volume
- 119
- Issue
- 2
- Pages
- 170-185
- ISSN
- 0301-4622 (ISSN-L)
- OpenAlex
- W2004262276
- Cited by
- 32
- References
- 54
- Citations by year
- 2025: 5 · 2024: 1 · 2022: 2 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 1 · 2014: 1 · 2012: 1
- FWCI
- 0.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biophysical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- apolipoprotein E, apolipoprotein E isoforms, protein stability, thermal denaturation, guanidine hydrochloride denaturation, multidomain structure, N-terminal domain, C-terminal domain, protein folding, recombinant protein
- MeSH terms
- Apolipoproteins E, Chromatography, Gel, Circular Dichroism, Humans, Particle Size, Protein Conformation, Sensitivity and Specificity, Solutions, Spectrometry, Fluorescence, Spectrophotometry, Ultraviolet, Temperature, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Guanidine, Apolipoprotein E3, Apolipoprotein E4, Apolipoprotein E2
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