Structural Insight Into a Human H Ferritin@Gold‐Monocarbene Adduct: Aurophilicity Revealed in a Biological Context

L Lucrezia Cosottini (Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy) A Andrea Giachetti (Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP) Sesto Fiorentino FI 50019 Italy) A Annalisa Guerri (Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy) A Ane Martinez‐Castillo (Structure and Cell Biology of Viruses Lab Center for Cooperative Research in Biosciences (CIC bioGUNE) Basque Research and Technology Alliance (BRTA) Derio Spain) A Andrea Geri (Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy) S Stefano Zineddu (Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy) N Nicola G. A. Abrescia (Structure and Cell Biology of Viruses Lab Center for Cooperative Research in Biosciences (CIC bioGUNE) Basque Research and Technology Alliance (BRTA) Derio Spain) L Luigi Messori (Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy) P Paola Turano A Antonio Rosato

Abstract

Abstract Human H ferritin (HuHf) has excellent potential as a nanocarrier for the selective delivery of anticancer metal‐based drugs to tumor cells. Here, we addressed the interaction of the gold monocarbene compound Au(NHC)Cl with HuHf by electrospray ionization‐mass spectrometry (ESI‐MS) measurements, which provide the metalation state of the protein subunits and demonstrate the involvement of protein cysteines in gold binding. The adduct between Au(NHC)Cl and HuHf was studied by cryo‐EM measurements, resulting in a high‐resolution 3D density map at 1.51 Å. The cryo‐EM structure shows a novel tetranuclear gold(I) cluster, located in a surface pocket of each subunit where it is bound to Cys90 and Cys102. The short inter‐metal distances are diagnostic of the occurrence of aurophilic interactions. The present work demonstrates the usefulness of cryo‐EM to investigate the interactions between metal‐based drugs and their protein targets/carriers, also leveraging the strong signal of transition metal ions.

Article Details

Volume / Issue Vol. 64, Issue 30
Published July 21, 2025
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (10)

L

Lucrezia Cosottini

Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy

A

Andrea Giachetti

Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP) Sesto Fiorentino FI 50019 Italy

A

Annalisa Guerri

Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy

A

Ane Martinez‐Castillo

Structure and Cell Biology of Viruses Lab Center for Cooperative Research in Biosciences (CIC bioGUNE) Basque Research and Technology Alliance (BRTA) Derio Spain

A

Andrea Geri

Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy

S

Stefano Zineddu

Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy

N

Nicola G. A. Abrescia

Structure and Cell Biology of Viruses Lab Center for Cooperative Research in Biosciences (CIC bioGUNE) Basque Research and Technology Alliance (BRTA) Derio Spain

L

Luigi Messori

Department of Chemistry “Ugo Schiff” University of Florence Via della Lastruccia 3–13 Sesto Fiorentino 50019 Italy

P

Paola Turano

A

Antonio Rosato