2. Academic Validation
  3. Phage-Display-Derived Peptide Binds to Human CD206 and Modeling Reveals a New Binding Site on the Receptor

Phage-Display-Derived Peptide Binds to Human CD206 and Modeling Reveals a New Binding Site on the Receptor

  • J Phys Chem B. 2019 Mar 7;123(9):1973-1982. doi: 10.1021/acs.jpcb.8b11876.
Eliana K Asciutto 1,  Sergei Kopanchuk 2,  Anni Lepland 3,  Lorena Simón-Gracia 3,  Carlos Aleman 4,  Tambet Teesalu 3 5 6,  Pablo Scodeller 3
Affiliations

Affiliations

  • 1 School of Science and Technology , National University of San Martin (UNSAM) and CONICET , Campus Migueletes, 25 de Mayo y Francia , CP 1650 San Martín , Buenos Aires , Argentina.
  • 2 Institute of Chemistry , University of Tartu , Ravila 14A , Tartu 50411 , Estonia.
  • 3 Laboratory of Cancer Biology, Institute of Biomedicine and Translational Medicine , University of Tartu , Ravila 14B , Tartu 50411 , Estonia.
  • 4 Departament d'Enginyeria Química and Barcelona Research Center in Multiscale Science and Engineering, EEBE , Universitat Politècnica de Catalunya , C/Eduard Maristany, 10-14 , 08019 Barcelona , Spain.
  • 5 Cancer Research Center , Sanford-Burnham-Prebys Medical Discovery Institute , 10901 North Torrey Pines Road , La Jolla , California 92037 , United States.
  • 6 Center for Nanomedicine and Department of Cell, Molecular and Developmental Biology , University of California, Santa Barbara Santa Barbara , California 93106 , United States.
PMID: 30768279 DOI: 10.1021/acs.jpcb.8b11876
Abstract

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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