Characterization of the Perilipin 5 11‐mer Region

Abstract

Lipid storage‐related diseases have become prevalent throughout the nation and are responsible for afflictions such as obesity and type II diabetes. Proteins such as the perilipin family serve a key role in the modulation of lipolysis. Although this protein family plays such a major role in biochemical processes, little information has been discovered pertaining to the structure of the Perilipins. Structure is central to understanding the function of a protein, and how that protein will interact will other molecules. There has been data showing the structure of the C‐terminal domain of perilipin 3; however, structural information for the other family members is yet, unknown. The current study is aimed to determine the structure of the 11‐mer region in Perilipin 5. The 11‐mer region is implicated in the interactions between Perilipin 5 and lipids. Bioinformatics data were obtained on the 11‐mer sequence. The secondary structure of the 11‐mer region was characterized using Phyre2, and RaptorX and viewed using molecular visualization software including PyMol and NGL. These models predicted the 11‐mer region to have an amphipathic alpha helix which allowed Perilipin 5 to bind to lipid droplets. Additional studies are being performed using protease protection assays and characterization of a synthetic peptide that mimics the 11‐mer region. Characterization on the 11‐mer region of Perilipin 5 will further help elucidate how this region of perilipin 5 associates with lipid droplets.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.