In situ ATR-IR spectroscopy study of adsorbed protein: Visible light denaturation of bovine serum albumin on TiO2

Bouhekka, Ahmed; Bürgi, Thomas

doi:10.1016/j.apsusc.2012.08.017

Cited by 89 publications

(66 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The authors describe the experimental set ups required and advantages of combining ATR FTIR with photochemistry, electrochemistry and perfusion to explore redox reactions, ligand binding and conversions between catalytic intermediates [30]. The useful combination of photochemistry and ATR FTIR spectroscopy was also recently demonstrated by Bouhekka & Bürgi [39]. In this study, the effect of visible light on BSA adsorbed onto TiO 2 particles was examined in-situ using multiple reflections ATR FTIR spectroscopy.…”

Section: Atr Ftir Spectroscopy Of Surfaces and Proteinsmentioning

confidence: 99%

Recent applications of ATR FTIR spectroscopy and imaging to proteins

Glassford¹,

Byrne²,

Kazarian³

2013

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

299

169

View full text Add to dashboard Cite

Attenuated Total Reflection (ATR) Fourier Transform Infrared (FTIR) spectroscopy is a label-free, non-destructive analytical technique that can be used extensively to study a wide variety of different molecules in a range of different conditions. The aim of this review is to discuss and highlight the recent advances in the applications of ATR FTIR spectroscopic imaging to proteins. It briefly covers the basic principles of ATR FTIR spectroscopy and ATR FTIR spectroscopic imaging as well as their advantages to the study of proteins compared to other techniques and other forms of FTIR spectroscopy. It will then go on to examine the advances that have been made within the field over the last several years, particularly the use of ATR FTIR spectroscopy for the understanding and development of protein interaction with surfaces. Additionally, the growing potential of Surface Enhanced Infrared spectroscopy (SEIRAS) within this area of applications will be discussed. The review includes the applications of ATR FTIR imaging to protein crystallization and for highthroughput studies, highlighting the future potential of the technology within the field of protein structural studies and beyond.

show abstract

Section: Atr Ftir Spectroscopy Of Surfaces and Proteinsmentioning

confidence: 99%

Recent applications of ATR FTIR spectroscopy and imaging to proteins

Glassford¹,

Byrne²,

Kazarian³

2013

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

299

169

View full text Add to dashboard Cite

show abstract

“…57 Bouhekka and B€ urgi noted that BSA adsorption on TiO 2 resulted in a decreased a-helix content to 23%. 24 Lehman et al reported a total a-helix content of 10% for BSA on nonporous SiO 2 and 12% on mesoporous SiO 2 , compared to 57% for BSA in solution. 40 Catalano et al reported an alpha helix content of approximately 36% for BSA adsorbed onto pyrolytic SiO 2 nanoparticles.…”

Section: Protein Secondary Structure As a Function Of Phmentioning

confidence: 99%

“…Most commonly, the alpha-helix content reported for BSA in aqueous media is 66%-68%. [24][25][26] However, it has been shown that under acidic conditions and/or upon adsorption, the alpha helical structure of BSA decreases. 13,27 The adsorption of proteins, including BSA, on nanoparticle surfaces has been investigated in terms of impacts on nanoparticle aggregation, protein coverage, and protein structure.…”

Section: Introductionmentioning

confidence: 99%

“…33,45 The amide I band has well characterized component bands of different frequencies corresponding to secondary protein structural motifs such as alpha helices. 13,24,28,40,43,44,[46][47][48] Additionally, the amide I peak will shift to lower wavenumbers when there are an increasing number of hydrogen bonds between the protein and the surface. 49 The frequencies of these absorbance bands may shift as a function of pH, and additional bands arise due to protonation/deprotonation of acidic and basic sites within the amino acid residues that make up the protein.…”

Section: Introductionmentioning

confidence: 99%

“…Then, spectra were curve fitted to a Gaussian-Lorentzian shape using five component peaks in the amide I region, determined from the second derivative spectra of the solution phase BSA and constrained by previous literature values. 13,24,46 Curve fitted spectra were further modified to have a linear baseline at zero in the amide I region and a peak maximum of exactly 1 absorbance unit in the amide I region.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

et al. 2017

View full text Add to dashboard Cite

Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO2) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO2 nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO2 nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO2 nanoparticles, whereas for SiO2 nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO2 complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO2 complex with a value of ca. 3 ± 1 × 1011 molecules cm−2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein–nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).

show abstract

An Underwater Surface‐Drying Peptide Inspired by a Mussel Adhesive Protein

Wei

Petrone

Tan

et al. 2016

Adv Funct Materials

183

168

View full text Add to dashboard Cite

Water hampers the formation of strong and durable bonds between adhesive polymers and solid surfaces, in turn hindering the development of adhesives for biomedical and marine applications. Inspired by mussel adhesion, a mussel foot protein homologue (mfp3S-pep) is designed, whose primary sequence is designed to mimic the pI, polyampholyte, and hydrophobic characteristics of the native protein. Noticeably, native protein and synthetic peptide exhibit similar abilities to self-coacervate at given pH and ionic strength. 3,4-dihydroxy-l-phenylalanine (Dopa) proves necessary for irreversible peptide adsorption to both TiO2 (anatase) and hydroxyapatite (HAP) surfaces, as confirmed by quartz crystal microbalance measurements, with the coacervate showing superior adsorption. The adsorption of Dopa-containing peptides is investigated by attenuated total reflection infrared spectroscopy, revealing initially bidentate coordinative bonds on TiO2, followed by H-bonded and eventually long-ranged electrostatic and Van der Waals interactions. On HAP, mfp3s-pep-3Dopa adsorption occurs predominantly via H-bond and outer-sphere complexes of the catechol groups. Importantly, only the Dopa-bearing compounds are able to remove interfacial water from the target surfaces, with the coacervate achieving the highest water displacement arising from its superior wetting properties. These findings provide an impetus for developing coacervated Dopa-functionalized peptides/polymers adhesive formulations for a variety of applications on wet polar surfaces.

show abstract

In situ ATR-IR spectroscopy study of adsorbed protein: Visible light denaturation of bovine serum albumin on TiO2

Cited by 89 publications

References 45 publications

Recent applications of ATR FTIR spectroscopy and imaging to proteins

Recent applications of ATR FTIR spectroscopy and imaging to proteins

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

An Underwater Surface‐Drying Peptide Inspired by a Mussel Adhesive Protein

Contact Info

Product

Resources

About