A Quantitative, Real-Time Assessment of Binding of Peptides and Proteins to Gold Surfaces

Ori Cohavi, Dana Reichmann, Renne Abramovich, Alexander B. Tesler, Giuliano Bellapadrona, Dania B. Kokh, Rebecca C. Wade, Alexander Vaskevich, Israel Rubinstein, Gideon Schreiber, Daria B. Kokh

Research output: Contribution to journalArticlepeer-review


Interactions of peptides and proteins with inorganic surfaces are important to both natural and artificial systems; however, a detailed understanding of such interactions is lacking. In this study, we applied new approaches to quantitatively measure the binding of amino acids and proteins to gold surfaces. Real-time surface plasmon resonance (SPR) measurements showed that TEM1-beta-lactamase inhibitor protein (BLIP) interacts only weakly with Au nanoparticles (NPs). However, fusion of three histidine residues to BLIP (3H-BLIP) resulted in a significant increase in the binding to the Au NPs, which further increased when the histidine tail was extended to six histidines (6H-BLIP). Further increasing the number of His residues had no effect on the binding. A parallel study using continuous (111)-textured Au surfaces and single-crystalline, (111)-oriented. Au islands by ellipsometry, FTIR, and localized surface plasmon resonance (LSPR) spectroscopy further confirmed the results, validating the broad applicability of Au NPs as model surfaces. Evaluating the binding of all other natural amino acid homo-tripeptides fused to BLIP (except Cys and Pro) showed that aromatic and positively-charged residues bind preferentially to Au with respect to small aliphatic and negatively charged residues, and that the rate of association is related to the potency of binding. The binding of all fusions was irreversible. These findings were substantiated by SPR measurements of synthesized, free, soluble tripeptides using Au-NP-modified SPR chips. Here, however, the binding was reversible allowing for determination of binding affinities that correlate with the binding potencies of the related BLIP fusions. Competition assays performed between 3H-BLIP and the histidine tripeptide (3 His) suggest that Au binding residues promote the adsorption of proteins on the surface, and by this facilitate the irreversible interaction of the polypeptide chain with Au. The binding of amino acids to Au w
Original languageEnglish
Pages (from-to)1327-1336
Number of pages10
JournalChemistry-A European Journal
Issue number4
StatePublished - 24 Jan 2011


  • gold
  • nanoparticles
  • proteins
  • surface chemistry
  • surface plasmon resonance

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Organic Chemistry


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