Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 123, Issue 9, Pages 1973-1982Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.8b11876
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Funding
- Agencia Nacional de Promocion Cientifica y Tecnologica grant [PICT-2015-1706]
- Estonian Research Council [PRG230, PSG38, IUT20-17]
- European Regional Development Fund [2014-2020.4.01.15-0012]
- European Research Council grant GLIOGUIDE from European Regional Development Fund
- European Regional Development Fund Mobilitas Plus postdoctoral fellowship MOBJD11
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We recently identified a tumor-homing peptide (mUNO, sequence: CSPGAK) that specifically interacts with mouse CD206 to target CD206/MRC1-expressing tumor-associated macrophages in mice. Here, we report studies on the binding of mUNO to human recombinant CD206 (hCD206) and on modeling the mUNO/hCD206 interaction by computational analysis. Fluorescence anisotropy analysis demonstrated that fluorophore-labeled mUNO interacts with hCD206. Microsecond time-scale molecular dynamics simulations and docking predictions showed that mUNO binds to a newly identified epitope between C-type lectin domains 1 and 2. The physical mechanisms that contribute to the docking interactions of mUNO include electrostatic interactions, aromatic interactions, and hydrogen bonds. We also demonstrate the selectivity of FAM-mUNO for CD206(+)-cultured human macrophages. The peptide mUNO appears to be the first ligand capable of interacting with this epitope of hCD206, for which no ligands have been reported. Our study has implications for targeting human M2-like tumor associated macrophages, a subpopulation of immune cells with a major protumoral role.
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