ATR-FTIR Study of IgG Adsorbed on Different Silica Surfaces

Giacomelli, Carla E.; Bremer, M.G.E.G.; Norde, Willem

doi:10.1006/jcis.1999.6479

Cited by 140 publications

(118 citation statements)

References 33 publications

(62 reference statements)

Supporting

Mentioning

109

Contrasting

Order By: Relevance

“…The interaction of proteins with silica surfaces has been studied using various spectroscopic techniques such as NMR, [9] IR-, [10] or ATR-IR spectroscopy. [11] Basiuk et al, [12] for example, suggested on the basis of IR spectroscopy that the formation of linear glycine oligomers is catalyzed by the silica surface through formation of a silica-glycine anhydride via an esterification reaction, as manifested by the appearance of an IR-absorption band at 1760 cm…”

Section: Introductionmentioning

confidence: 99%

Investigating Alanine–Silica Interaction by Means of First‐Principles Molecular‐Dynamics Simulations

Nonella

Seeger

2008

ChemPhysChem

View full text Add to dashboard Cite

In our attempts to achieve a detailed understanding of protein-silica interactions at an atomic level we have, as a first step, simulated a small system consisting of one alanine in different protonation states, and a hydroxylated silica surface, using a first-principles molecular-dynamics technique. The simulations are carried out in vacuo as well as in the presence of water molecules. In the case of a negatively charged surface and an alanine cation, an indirect proton transfer from the alanine carboxylic group to the surface takes place. The transfer involves several water molecules revealing an alanine in its zwitterionic state interacting with the neutral surface through indirect hydrogen bonds mediated by water molecules. During the simulation of the zwitterionic state the ammonium group eventually establishes a direct -N-H...O-Si interaction, suggesting that the surface-amino group interaction is stronger than the interaction between the surface and the carboxylic group. In vacuum simulations, the amino group exhibits clearly stronger interactions with the surface than the carboxylic group.

show abstract

Section: Introductionmentioning

confidence: 99%

Investigating Alanine–Silica Interaction by Means of First‐Principles Molecular‐Dynamics Simulations

Nonella

Seeger

2008

ChemPhysChem

View full text Add to dashboard Cite

show abstract

“…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. [27][28][29][30][31][32][33] Investigations on the effects of pH have been conducted and shown that protein adsorption is the greatest at or near the isoelectric point, [34][35][36][37] and there is not necessarily a pH-dependent trend for protein adsorption to nanoparticle surfaces away from the isoelectric point. 37 Aggarwal et al conducted a study on pure silica and zirconia nanoparticle surfaces and a mixture of nanoparticle surfaces and found that the composite surface better retains the native protein structure upon adsorption.…”

Section: Introductionmentioning

confidence: 99%

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

“…Although AFM works at ambient temperature, even in liquid the surface is visualized only over a very small area [7,8,[10][11][12]. FTIR is suitable only for micro-samples, allowing the molecular bond and grouping vibrations to be deducted [7,[13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Inhibitory effect of common microfluidic materials on PCR outcome

Kodzius

Xiao

et al. 2012

Sensors and Actuators B: Chemical

View full text Add to dashboard Cite

a b s t r a c tIn this study, we established a simple method for evaluating the PCR compatibility of various common materials employed when fabricating microfluidic chips, including silicon, several kinds of silicon oxide, glasses, plastics, wax, and adhesives. Two-temperature PCR was performed with these materials to determine their PCR-inhibitory effect. In most cases, adding bovine serum albumin effectively improved the reaction yield. We also studied the individual PCR components from the standpoint of adsorption. Most of the materials did not inhibit the DNA, although they noticeably interacted with the polymerase. We provide a simple method of performing PCR-compatibility testing of materials using inexpensive instrumentation that is common in molecular biology laboratories. Furthermore, our method is direct, being performed under actual PCR conditions with high temperature. Our results provide an overview of materials that are PCR-friendly for fabricating microfluidic devices. The PCR reaction, without any additives, performed best with pyrex glass, and it performed worst with PMMA or acrylic glue materials.

show abstract

ATR-FTIR Study of IgG Adsorbed on Different Silica Surfaces

Cited by 140 publications

References 33 publications

Investigating Alanine–Silica Interaction by Means of First‐Principles Molecular‐Dynamics Simulations

Investigating Alanine–Silica Interaction by Means of First‐Principles Molecular‐Dynamics Simulations

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

Inhibitory effect of common microfluidic materials on PCR outcome

Contact Info

Product

Resources

About