ArticleAntibody therapeutics2026
Fully human antagonistic antibodies targeting FPR2 through dual extracellular-loop engagement for gastric cancer therapy.
Article in Antibody therapeutics, 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
Background: Gastric cancer (GC) remains a major cause of cancer mortality worldwide, particularly in metastatic stages. N-formyl peptide receptor 2 (FPR2), a class A G protein-coupled receptor activated by the Methods: We generated fully human antagonistic antibodies targeting FPR2 using a two-step discovery strategy. A CDR-H3-focused synthetic single-chain variable fragment library was screened against an extracellular loop 3 (ECL3) peptide, followed by light-chain engineering to confer dual engagement of extracellular loop 2 (ECL2). Results: The engineered antibody exhibited dose-dependent binding to both ECL2 and ECL3 peptides, selectively recognized FPR2 over other FPR family members, and showed nanomolar binding to FPR2-expressing cancer cells. The antibody inhibited Hp(2-20)-induced calcium mobilization and suppressed migration and invasion of Adenocarcinoma Gastric (AGS) gastric cancer cells. Structural modeling indicated a lid-like binding mode occluding the orthosteric pocket. Conclusions: We developed a fully human antagonistic antibody that selectively binds and inhibits FPR2 through dual extracellular-loop engagement. The antibody potentially suppresses FPR2-driven signaling and invasive behaviors in gastric cancer cells, supporting its development for therapeutic application. Further assessment of its efficacy
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