In Situ Monitoring of Protein Adsorption on a Nanoparticulated Gold Film by Attenuated Total Reflection Surface-Enhanced Infrared Absorption Spectroscopy

Jin, Bo; Bao, Wenjing; Wu, Zeng-Qiang; Xia, Xing‐Hua

doi:10.1021/la300819u

Cited by 34 publications

(45 citation statements)

References 54 publications

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“…Protein adsorption on AuNP has been reported to deviate from simple Langmuir adsorption previously. 3,25 It is likely that hemoglobin forms at least partial multilayers already at the comparatively low protein concentrations used here. 26 Multilayer formation explains why the BET isotherm provides the best fit of our protein adsorption data ( Figure 4).…”

Section: Hemoglobin Layer Structurementioning

confidence: 96%

Formation Mechanism for Stable Hybrid Clusters of Proteins and Nanoparticles

et al. 2015

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Citrate-stabilized gold nanoparticles (AuNP) agglomerate in the presence of hemoglobin (Hb) at acidic pH. The extent of agglomeration strongly depends on the concentration ratio [Hb]/[AuNP]. Negligible agglomeration occurs at very low and very high [Hb]/[AuNP]. Full agglomeration and precipitation occur at [Hb]/[AuNP] corresponding to an Hb monolayer on the AuNP. Ratios above and below this value lead to the formation of an unexpected phase: stable, microscopic AuNP-Hb agglomerates. We investigated the kinetics of agglomeration with dynamic light scattering and the adsorption kinetics of Hb on planar gold with surface-acoustic wave-phase measurements. Comparing agglomeration and adsorption kinetics leads to an explanation of the complex behavior of this nanoparticle-protein mixture. Agglomeration is initiated either when Hb bridges AuNP or when the electrostatic repulsion between AuNP is neutralized by Hb. It is terminated when Hb has been depleted or when Hb forms multilayers on the agglomerates that stabilize microscopic clusters indefinitely.

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Section: Hemoglobin Layer Structurementioning

confidence: 96%

Formation Mechanism for Stable Hybrid Clusters of Proteins and Nanoparticles

et al. 2015

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“…Adsorption of hemoglobin (Hb) on naked gold nanoparticles or SAM-modified gold electrodes was studied by monitoring the time resolved evolution of amide signals [69,70]. Results showed that both the electrostatic interaction and the coordination bonds between bovine hemoglobin (BHb) residues and Au NP film surface affected the adsorption kinetics.…”

Section: Adsorption and Conformation Changesmentioning

confidence: 99%

“…The maximum adsorption was obtained at solution pH 7.0. Due to these irreversible interactions and non-uniformed surface structure of gold nanoparticles, the adsorption process of BHb on gold nanoparticle film can be better described by the Freundlich adsorption equation [69]. The immobilization of Hb on PO 3 H 2 -terminated SAMs followed a relatively sluggish process due to the formation of multilayer Hb structures [70].…”

Section: Adsorption and Conformation Changesmentioning

confidence: 99%

Attenuated Total Reflection Surface-Enhanced Infrared Absorption Spectroscopy: a Powerful Technique for Bioanalysis

Zhang

et al. 2017

J. Anal. Test.

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Attenuated total reflection surface-enhanced infrared absorption spectroscopy (ATR-SEIRAS) has recently been proven to be a powerful tool for bioanalysis. It enables in situ and in real-time observation of dynamic processes occurring on specific interface, revealing rich structural and functional information of biomolecules at sub monolayer level. The aim of this general review was to give an overview of the cutting edge applications of ATR-SEIRAS. We start with description of the basic configuration of the standard ATR-SEIRAS platform. The enhanced mechanisms and methods to fabricate enhanced substrates are then presented. We discuss the recent developments, challenges and applications of ATR-SEIRAS in bioanalysis, mainly focusing on DNA analysis, protein behavior and cell properties. Finally, further development of the ATR-SEIRAS technique with enhanced sensitivity, improved time and spatial resolutions will be prospected.

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“…Surface-enhanced infrared adsorption spectroscopy (SEIRAS) is an effective detection method to study the secondary structure of proteins in a super-thin layer adsorbed onto a nano-Au film [13][14][15]. The vibration of the adsorbed molecules or proteins can be enhanced by more than 2 orders of magnitude, which solves the problem in poor sensitivity of conventional IR spectroscopy.…”

mentioning

confidence: 99%

“…Moreover, SEIRAS not only can in-situ and real-time monitor adsorption of proteins onto biomimic membranes [13,15,16], but also can detect the change in the adsorption properties of proteins and biomimic membranes induced by interaction with nanoparticles [17]. By combining with electrochemistry, potential-induced SEIRA difference spectroscopy can finely reflect some very small changes of the secondary structure and component groups of redox proteins during the process of electron acceptance and donation [12,18].…”

mentioning

confidence: 99%

Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface

Zhang

Zeng

Liu

et al. 2016

Electrochimica Acta

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Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface, Electrochimica Acta http://dx. AbstractStudy of the interactions between engineered nanoparticles and biomolecules plays an important role in understanding nano-bio effect. However, most of studies focus on the interaction of protein with nanoparticle in bulk phase, the impact of nanoparticle on the function of protein immobilized on the biological interface has been ignored for a long time. In this paper, we study the effect of SiO2 NPs on electron transfer function of cytochrome c (cyt c) adsorbed onto the 11-mercaptoundecanoic acid (MUA) self-assembled monolayer (SAM) by surface-enhanced infrared absorption spectroscopy (SEIRAS) combined with electrochemistry. Our results disclose that instead of inhibiting the electron transfer, exposure of SiO2 NPs enhances the redox reversibility, electron transfer rate, and catalytic performance of adsorbed cyt c, but induces a slight negative shift in the formal potential of the adsorbed cyt c. Interaction of SiO2 NPs slightly induces the structural changes of the β-sheet in the oxidized form and the change of microenvironment surrounding them, which could further change the microenvironment and the orientation of heme, facilitating the hydration of cyt c at the oxidized state. It could be the enhanced hydration of cyt c (Fe 3+ ) and a smaller change in the total hydration from reduced to oxidized state that results in the slight negative shift in the formal potential and promotes the electron transfer capability. Besides, cyt c's slight conformational change and the disturbance to the microenvironment of heme resulting from the adsorption of SiO2 NPs could also be one of the reason that leads to the enhanced catalytic capability towards the reduction of H2O2.

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In Situ Monitoring of Protein Adsorption on a Nanoparticulated Gold Film by Attenuated Total Reflection Surface-Enhanced Infrared Absorption Spectroscopy

Cited by 34 publications

References 54 publications

Formation Mechanism for Stable Hybrid Clusters of Proteins and Nanoparticles

Formation Mechanism for Stable Hybrid Clusters of Proteins and Nanoparticles

Attenuated Total Reflection Surface-Enhanced Infrared Absorption Spectroscopy: a Powerful Technique for Bioanalysis

Surface-enhanced infrared absorption spectroscopy and electrochemistry reveal the impact of nanoparticles on the function of protein immobilized on mimic biointerface

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