Differential interaction of peptides derived from C-terminal domain of human apolipoprotein E with platelet activating factor analogs |
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Authors: | Sunil A Nankar Priyanka BajajRevuri Sravanthi Abhay H Pande |
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Institution: | Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, Mohali 160062, Punjab, India |
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Abstract: | Apolipoprotein-derived peptides are promising candidates for the treatment of various inflammatory conditions and the main mechanism proposed for the protective action of these peptides includes binding to pro-inflammatory lipid mediators with high affinity and facilitating their sequestration/metabolism/clearance in the body. Molecules that act as pro-inflammatory lipid mediators differ considerably in their molecular structures, chemical compositions and physicochemical properties. Importance of the properties of pro-inflammatory lipid mediators on the biological activity of apolipoprotein-derived peptides has not been studied in detail. In this study, we characterized the physicochemical properties of aggregates containing lyso-PAF, acetyl-PAF and butanoyl-PAF, three closely related pro-inflammatory lipid mediators, and studied their interaction with peptides derived from the C-terminal domains of human apolipoprotein E. These PAF-analogs differ only in the chemical composition of the functional groups they carry at the sn-2 positions. Our results show that physicochemical properties of aggregates containing lyso-PAF, acetyl-PAF and butanoyl-PAF differ considerably and affect their apolipoprotein-derived peptides-binding capacity. |
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Keywords: | Apolipoprotein-derived peptide Acetyl-PAF Lyso-PAF Butanoyl-PAF Circular dichroism qRT-PCR ELISA Fluorescence spectroscopy |
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