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Human plasma low density lipoprotein: a fluorescence study

S Singh¹, J Gupta

¹Division of Biopolymers, Central Drug Research Institute, Lucknow.

Indian Journal of Biochemistry & Biophysics

|June 1, 1993

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Human plasma low-density lipoprotein (LDL) surfaces are hydrophobic. Fluorescence spectroscopy revealed specific binding sites for 8-anilino-1-naphthalene sulfonate (ANS) on LDL, indicating a nonpolar environment.

Area of Science:

Biochemistry
Spectroscopy
Lipidology

Background:

Human plasma low-density lipoprotein (LDL) plays a crucial role in lipid transport.
The surface properties of LDL, particularly its hydrophobicity, are critical for its function and interactions.
Understanding LDL surface characteristics is essential for comprehending lipoprotein metabolism and associated diseases.

Purpose of the Study:

To investigate the hydrophobic nature of the human plasma low-density lipoprotein (LDL) surface.
To characterize the binding sites and interactions of 8-anilino-1-naphthalene sulfonate (ANS) on LDL.
To elucidate the conformational changes occurring on the LDL surface upon ANS binding.

Main Methods:

Fluorescence spectroscopy was employed to study the hydrophobic properties of LDL.

Related Experiment Videos

The binding of 8-anilino-1-naphthalene sulfonate (ANS) to LDL was quantified using fluorescence measurements.

Temperature-dependent studies were conducted to assess the stability of LDL-ANS interactions.

Protein fluorescence quenching was used to detect energy transfer and conformational changes.

Main Results:

A significant enhancement in ANS fluorescence quantum yield (0.004 to 0.114 at 470 nm) indicated low polarity of ANS binding sites on LDL.
LDL possesses 77 homogeneous binding sites for ANS with an association constant (Ka) of 2.5 x 10^5 M^-1.
Temperature variations (15-45°C) did not affect the number of binding sites or the association constant.
Quenching of protein fluorescence suggested energy transfer in the LDL-ANS complex, implying conformational changes and proximity of charge acceptor segments to ANS sites.
A ~30-fold increase in ANS quantum yield and a large shift in emission maximum confirmed a highly hydrophobic surface environment on LDL particles.

Conclusions:

The surface of human plasma LDL exhibits a significantly hydrophobic character.
ANS binds to a homogeneous set of sites on LDL, with binding being independent of temperature within the studied range.
Conformational changes occur on the LDL surface upon ANS binding, leading to increased hydrophobicity and energy transfer.