ArticleCellular & molecular biology letters2026
Targeting biglycan-TLR2/TLR4 interaction with synthetic peptides mitigates inflammation and ameliorates renal function in ischemia-reperfusion injury.
Article in Cellular & molecular biology letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundRenal ischemia-reperfusion injury (IRI), characterized by enhanced inflammation, is a leading cause of acute kidney injury (AKI) with limited treatments beyond supportive dialysis. Biglycan through toll-like receptors (TLR)2/TLR4 signaling aggravates tissue damage in acute renal IRI. This study aimed to identify the TLR2/TLR4 binding sites of biglycan and test the efficacy of biglycan-derived peptides in vitro and in vivo.
methodsEpitope mapping was conducted using PepSpot peptide arrays with overlapping 15-mer biglycan peptides. Binding of wildtype (WT) and mutant biglycan proteins and synthesized peptides to TLR2 and TLR4 was analyzed by microscale thermophoresis. Nuclear Factor (NF)-κB activation was assessed in HEK-Blue-TLR2 and HEK-Blue-TLR4 reporter cells following stimulation with biglycan variants and peptides. Primary murine and human monocyte-derived macrophages were used to evaluate inflammatory responses in vitro. Renal IRI was induced in C57BL/6 mice with intravenous peptide treatment administered prior to surgery. Renal function, immune cell infiltration, and cytokine expression were assessed using serum creatinine measurements, immunohistochemistry, and molecular analyses.
resultsPepSpot epitope mapping identified
conclusionsThe findings delineate conserved biglycan-TLR2/TLR4 recognition sequences and design of inhibitory peptides with therapeutic efficacy in vitro and in vivo. Peptides that inhibit biglycan-TLR2/TLR4 binding offer a targeted therapeutic approach for mitigating biglycan-TLR-associated sterile and pathogen-induced inflammatory diseases, with significant translational relevance for IRI.
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