<br/>Specific peptides are a means of selectively targeting receptors upregulated in cancerous cells. In this work, we designed several polyphenol-peptide conjugates utilizing peptide sequences obtained from phage display library. The conjugates were specifically designed to target breast cancer. Ten different conjugates were designed to examine specificity toward Ephrin receptors (EphB4 and EphB2) as well as estrogen receptors. We generated several conjugates through point mutations of the original sequence to test their ability to bind to the receptor and analyze differences in binding interactions within the active site. Models were created on ChemDraw and optimized on Chem3D. Structures were visualized on PyMol and thermodynamic calculations were performed using Turbomole and COSMOS-RS. We performed studies to predict the active site of the receptor and compared this to the results of docking studies using Metapocket and PLIP. The bioactivity, solubility, absorption, distribution, metabolism, excretion, and toxicity properties of the dipeptides and tripeptides were then predicted using SwissADME. Comparisons of the conjugates indicate that inducing a mutation at in the original peptide sequence could improve the targeting and binding at the receptors and thus serve as potential candidates for targeting breast cancer.

Physicochemical properties, molecular docking of polyphenols derivatized with in silico targeted peptides, and their potential as drug candidates.

ACS Spring Meeting 2021

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.