TY - JOUR
T1 - A Quantitative, Real-Time Assessment of Binding of Peptides and Proteins to Gold Surfaces
AU - Cohavi, Ori
AU - Reichmann, Dana
AU - Abramovich, Renne
AU - Tesler, Alexander B.
AU - Bellapadrona, Giuliano
AU - Kokh, Dania B.
AU - Wade, Rebecca C.
AU - Vaskevich, Alexander
AU - Rubinstein, Israel
AU - Schreiber, Gideon
AU - Kokh, Daria B.
N1 - EU [028331]; Israel Science Foundation [672/07]; Klaus Tschira FoundationSupport of this work by EU NEST project PROSURF, No. 028331, is gratefully acknowledged. A.V. and I.R. acknowledge support by the Israel Science Foundation, grant No. 672/07. This research is made possible in part by the historic generosity of the Harold Perlman family. We thank the BioRad team in Haifa (Israel) for their supply of materials and technical support for the experiments. We thank the Israel Structural Proteomics Center (WIS) for their generous gift of purified proteins. D.K. and R.C.W. gratefully acknowledge the support of the Klaus Tschira Foundation.
PY - 2011/1/24
Y1 - 2011/1/24
N2 - 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
AB - 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
KW - gold
KW - nanoparticles
KW - proteins
KW - surface chemistry
KW - surface plasmon resonance
UR - http://www.scopus.com/inward/record.url?scp=78751611891&partnerID=8YFLogxK
U2 - https://doi.org/10.1002/chem.201001781
DO - https://doi.org/10.1002/chem.201001781
M3 - مقالة
C2 - 21243701
SN - 0947-6539
VL - 17
SP - 1327
EP - 1336
JO - Chemistry-A European Journal
JF - Chemistry-A European Journal
IS - 4
ER -