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Proinflammatory Action of a New Electronegative Low-Density Lipoprotein Epitope

Faulin, Tanize do Espirito Santo; Kazuma, Soraya Megumi; Tripodi, Gustavo Luis; Cavalcante, Marcela Frota; Wakasuqui, Felipe; Oliveira, Cristiano Luis Pinto; Degenhardt, Maximilia Frazão de Souza; Michaloski, Jussara; Giordano, Ricardo José; Ketelhuth, Daniel Francisco Jacon; Abdalla, Dulcineia Saes Parra

By 27 January 2020March 17th, 2021No Comments

Biomolecules, 2019, vol 9, 8,



The electronegative low-density lipoprotein, LDL (−), is an endogenously modified LDL subfraction with cytotoxic and proinflammatory actions on endothelial cells, monocytes, and macrophages contributing to the progression of atherosclerosis. In this study, epitopes of LDL (−) were mapped using a phage display library of peptides and monoclonal antibodies reactive to this modified lipoprotein. Two different peptide libraries (X6 and CX8C for 6- and 8-amino acid-long peptides, respectively) were used in the mapping. Among all tested peptides, two circular peptides, P1A3 and P2C7, were selected based on their high affinities for the monoclonal antibodies. Small-angle X-ray scattering analysis confirmed their structures as circular rings. P1A3 or P2C7 were quickly internalized by bone marrow-derived murine macrophages as shown by confocal microscopy. P2C7 increased the expression of TNFα, IL-1 β and iNOS as well as the secretion of TNFα, CCL2, and nitric oxide by murine macrophages, similar to the responses induced by LDL (−), although less intense. In contrast, P1A3 did not show pro-inflammatory effects. We identified a mimetic epitope associated with LDL (−), the P2C7 circular peptide, that activates macrophages. Our data suggest that this conformational epitope represents an important danger-associated molecular pattern of LDL (−) that triggers proinflammatory responses.

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