The physical state of the LDL core influences the conformation of apolipoprotein B-100 on the lipoprotein surface

We assessed the influence of temperature on the secondary structure of apolipoprotein B-100 (apoB) in normal low-density lipoprotein (N-LDL) and triglyceride-rich LDL (T-LDL). Gradual heating from 7°C to the phase-transition temperature of the lipoprotein core (∼28°C and ∼15°C for N-LDL and T-LDL, r...

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Bibliographic Details
Published in:FEBS letters 2003-01, Vol.533 (1), p.21-24
Main Authors: Coronado-Gray, Andrea, van Antwerpen, Rik
Format: Article
Language:English
Subjects:
Apolipoprotein B-100
Apolipoproteins B - chemistry
Calorimetry, Differential Scanning
Chemical Phenomena
Chemistry, Physical
Cholesteryl ester
Circular Dichroism
Circular dichroism spectroscopy
Differential scanning calorimetry
Humans
In Vitro Techniques
Lipoproteins, LDL - chemistry
Liquid state
Liquid-crystalline state
Protein Conformation
Protein Structure, Secondary
Thermodynamics
Triglycerides - chemistry
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Summary:We assessed the influence of temperature on the secondary structure of apolipoprotein B-100 (apoB) in normal low-density lipoprotein (N-LDL) and triglyceride-rich LDL (T-LDL). Gradual heating from 7°C to the phase-transition temperature of the lipoprotein core (∼28°C and ∼15°C for N-LDL and T-LDL, respectively) gradually altered the secondary structure of apoB, while further heating from the phase-transition temperature to 45°C had no additional effect. Above the phase-transition temperature of the core, the apoBs of N-LDL and T-LDL had a similar secondary structure. These results indicate that the conformation of apoB on the LDL surface depends strongly on the physical state of the lipoprotein core, and less on the lipid composition of the core per se.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)03731-6