Binding of silver nanoparticles to bacterial proteins depends on surface modifications and inhibits enzymatic activity.
Here we describe results from a proteomic study of protein-nanoparticle interactions to further the understanding of the ecotoxicological impact of silver nanoparticles (AgNPs) in the environment. We identified a number of proteins from Escherichia coli that bind specifically to bare or carbonate-coated AgNPs. Of these proteins, tryptophanase (TNase) was observed to have an especially high affinity for both surface modifications despite its low abundance in E. coli. Purified TNase loses enzymatic activity upon associating with AgNPs, suggesting that the active site may be in the vicinity of the binding site(s). TNase fragments with high affinities for both types of AgNPs were identified using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. Differences in peptide abundance/presence in mass spectra for the two types of AgNPs suggest preferential binding of some protein fragments based on surface coating. One high-binding protein fragment contained a residue (Arg103) that is part of the active site. Ag adducts were identified for some fragments and found to be characteristic of strong binding to AgNPs rather than association of the fragments with ionic silver. These results suggest a probable mechanism for adhesion of proteins to the most commonly used commercial nanoparticles and highlight the potential effect of nanoparticle surface coating on bioavailability.
Environmental Microbiology Laboratory, Ecole Polytechnique Federale de Lausanne, CH-1015 Lausanne, Switzerland.
Nicholas S
NS
Wigginton
Alexandre
A
de Titta
Flavio
F
Piccapietra
Jan
J
Dobias
Victor J
VJ
Nesatyy
Marc J F
MJ
Suter
Rizlan
R
Bernier-Latmani
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism* / Q000502:physiology; D053768:Metal Nanoparticles / Q000737:chemistry* / Q000633:toxicity; D011485:Protein Binding / Q000187:drug effects; D012834:Silver / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D013499:Surface Properties; D014368:Tryptophanase / Q000037:antagonists & inhibitors / Q000378:metabolism
D001426:Bacterial Proteins; D012834:Silver; D014368:Tryptophanase