Previous Page  14 / 22 Next Page
Information
Show Menu
Previous Page 14 / 22 Next Page
Page Background

Notes:

Page 48

Analytica 2016

September 28-30, 2016

Volume 7, Issue 5(Suppl)

J Anal Bioanal Tech 2016

ISSN: 2155-9872 JABT, an open access journal

conferenceseries

.com

September 28-30, 2016 Orlando, USA

7

th

International Conference and Exhibition on

Analytical & Bioanalytical Techniques

Shobini Jayaraman, J Anal Bioanal Tech 2016, 7:5(Suppl)

http://dx.doi.org/10.4172/2155-9872.C1.024

Comprehensive overview of biophysical studies of lipoprotein stability

Shobini Jayaraman

Boston University School of Medicine, USA

L

ipoproteins are nanoparticles comprised of proteins and lipids that provide vehicles for transport of fat and cholesterol in

circulation. High levels of certain lipoproteins increase the risk of heart disease. Each lipoprotein is a non-covalent assembly

of several proteins and several hundred lipids. The major challenge in the biophysical analysis of lipoproteins arises from their

heterogeneity in size (7-100 nm), density (1.06-1.22 g/L), and protein and lipid composition. Moreover, lipoproteins are highly

dynamic assemblies undergoing continuous remodeling via various enzymatic and non-enzymatic reactions. This provides a

major challenge for detailed structural studies of lipoproteins. To overcome this challenge, we designed an integrated biophysical

approach by combining far- and near-UV circular dichroism (CD) spectroscopy, turbidity, differential scanning calorimetry

(DSC), fluorescence spectroscopy, transmission electron microscopy (EM), size-exclusion chromatography (SEC) and other

methods to analyze the structure and remodeling of all major lipoprotein classes. This integrated approach was used to study

thermal denaturation of human low- and high-density lipoproteins (LDL and HDL, or bad and good cholesterol). The results

clearly showed that lipoprotein stability is controlled by kinetics barriers. Interestingly, heat-induced remodeling of all lipoproteins

involves partial protein unfolding/dissociation and lipoprotein fusion and rupture. These structural transitions mimic key aspects

of

in vivo

lipoprotein remodeling. These and other emerging approaches will allow one to study structural, dynamic and functional

properties of larger more challenging systems. Ultimately, such integrated approaches are hoped to bridge the gap between the

biophysical studies of isolated macromolecules or their complexes, and the complexity of cellular systems.

Biography

Shobini Jayaraman has completed her PhD from Indian Institute of Technology Madras, India and Post-doctoral studies from Weizmann Institute of Science, Israel.

She was the recipient of Sir Charles Clore Fellowship at Weizmann Institute of Science. Currently, she is a Senior Research Scientist at Boston University School of

Medicine. She serves as the liaison for academic and industrial contract research services at Boston University. She has published more than 25 papers in reputed

journals. Her recent publication in

JBC

has been chosen as paper of the month in May-2014 by International Atherosclerosis Society.

shobini@bu.edu