Previous Page  7 / 24 Next Page
Information
Show Menu
Previous Page 7 / 24 Next Page
Page Background

Page 49

Notes:

Journal of Pharmaceutical care and Health Systems | ISSN: 2376-0419 | Volume 5

Pharmaceutical sciences

11

th

World Congress on

September 28-29, 2018 | Montreal, Canada

Bioinformatic tools for determination of high-affinity peptides as alternative to treatment of Obesity

Ivonne M Bartsch, Sergio Marshall, Fanny Guzman Q

and

Constanza Cardenas C

Pontifical Catholic University of Valparaíso, Chile

O

psonin C3b is an important part of the immune system, being able to trigger phagocytosis by binding to the complement

receptors (CR1) of macrophages. The coating of cells with C3b positions them at risk of destruction. The AQP7 protein

is highly specific in adipocytes, therefore they can be targets for the generation of the dual agonist of adipose cells and CR1,

through hybrid peptides for the activation of the phagocytosis of the former. In this work, we will perform a bioinformatic

analysis through the design of peptides, based on these sequences to trigger phagocytosis adipocytes as an alternative to obesity

treatment. Materials and Methods: For the development of this work, we used UniProt, Ncbi Protein Blast, and PDBsum as

databases, Patchdock and FireDock for the realization of the Docking and I-Tasser for the modeling of the AQP7 protein; All

of them of free access. To analyze if there is a binding between peptides and AQP7 protein, it was used fibroblast 3T3-L1 cell

line and differentiated into adipocytes. To analyze if peptides bind to the CR1 protein, it was used THP-1 monocytes cell line.

Conclusions: From the interaction sites between C3b and CR1 it was possible to obtain four receptor agonist peptides. From

the modeling and subsequent docking between AQP7 and other protein structures (IgG) were found six binding peptides. For

the design of the hybrid peptides, a matrix was generated with 36 resulting peptides capable of binding to CR1 to AQP7. Of

these peptides, two are capable to bind to AQP7 and two binds to CR1. The final matrix of 4 peptides needs to be proved by a

co-culture of this two cell lines and demonstrate phagocytosis activation.

Biography

Ivonne Bartsch is a B.S. Pharmacist and PhD Biotechnology student at the Pontifical Catholic University of Valparaiso, Chile. From 2008 to 2013: founder and

director of a private Quality Control Drugs laboratory (Bioeq). Diplomate in Pharmaceutical Management and a Post-title Care Pharmacy at the University of

Valparaiso. Since 2013, Auxiliar Professor Quality Control, Medical School in Andrés Bello University, Vina del Mar, Chile. Presenter in XL annual meeting of the

society of Biochemistry and Molecular Biology, Chile.

Ivonne M Bartsch et al., J Pharma Care Health Sys 2018, Volume 5

DOI: 10.4172/2376-0419-C3-033