New Insights into the Biophysical Behavior of an Old Molecule: Experimental and Theoretical Studies of the Interaction Between 1,10-Phenanthroline and Model Phospholipid Membranes

Author(s)

Alvarez, Natalia ; Freddi, Priscilla ; Castellani, Stephanie ; Veiga, Nicolas ; Facchin, Gianella ; Costa-Filho, Antonio J.

• Document type: Journal article
• Source: Brazilian Journal of Physics; v. 52, n. 4, p. 8-pg., 2022-08-01.

Abstract

1,10-Phenanthroline, phen, is a molecule with a wide variety of chemical and biological activities, being interesting from a pharmacological standpoint. Its metal complexes have been extensively studied during the last century. Considering the vast applications of phen and its metallic complexes for the development of potential metallodrugs, it becomes of utmost importance to study the molecule's interaction with different molecular targets. So far, in-depth analyses of phen and metal-phen complexes' interaction with DNA are abundant. Nevertheless, little has been reported on the interaction of this molecule with the first molecular "target" that it finds in the cell, the lipid membrane. Here, we present the characterization of the interaction of the phen molecule with model membranes of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1,2-dipalmitoyl-sn-glycero-3-phospho-(1 '-rac-glycerol) (sodium salt) (DPPG) using a combination of differential scanning calorimetry and molecular dynamics simulations. Our results indicate that phen diffuses into the membranes, being stabilized around the middle of the hydrocarbon chains in DPPC, while in DPPG, it is placed near the center of the bilayer. (AU)

• FAPESP's process: 15/50366-7 - Resolving mechanistic details of peptide transport across membranes using crystallographic and non-crystallographic structural biology approaches
• Grantee: Antonio José da Costa Filho
• Support Opportunities: Regular Research Grants
• FAPESP's process: 20/15542-7 - Design and characterization of micro-reactors constituted by the protein chlorocatechol 1,2-dioxygenase and low complexity domains
• Grantee: Antonio José da Costa Filho
• Support Opportunities: Regular Research Grants