Concanavalin A and Polysaccharide on Gold Surfaces

Debono, Reno; Krull, Ulrich J.; Rounaghi, G. H.

doi:10.1021/bk-1992-0511.ch011

Cited by 5 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been reported that the adsorption of Con A on bare gold is less when the cofactors Ca 2+ and Mn 2+ are present. [100] It has also been reported that Con A is denatured upon interaction with bare Au surfaces. While our mixed monolayer are resistive and show well-formed semicircles in the Nyquist plots, the presence of some patches of bare Au cannot be ruled out.…”

Section: Discussionmentioning

confidence: 99%

Comparative Study of the Binding of Concanavalin A to Self-Assembled Monolayers Containing a Thiolated α-Mannoside on Flat Gold and on Nanoporous Gold

Pandey

Tan

Fujikawa

et al. 2012

Journal of Carbohydrate Chemistry

View full text Add to dashboard Cite

We have prepared SAMs containing 8-mercaptooctyl α-D-mannopyranoside, either as a single component or in mixed SAMs with n-octanethiol on flat gold surfaces and on nanoporous gold. Electrochemical impedance spectroscopy showed that the mixed SAMs on flat gold surfaces showed the highest Con A binding near 1:9 solution molar ratio of thiolatedα-mannoside to n-octanethiol whereas those on NPG showed the highest response at 1:19 solution molar ratio of thiolated α-mannoside to n-octanethiol. Atomic force microscopy was employed to image the monolayers, and also to image the bound Con A protein.

show abstract

Section: Discussionmentioning

confidence: 99%

Comparative Study of the Binding of Concanavalin A to Self-Assembled Monolayers Containing a Thiolated α-Mannoside on Flat Gold and on Nanoporous Gold

Pandey

Tan

Fujikawa

et al. 2012

Journal of Carbohydrate Chemistry

View full text Add to dashboard Cite

show abstract

“…This result suggests that direct adsorption of Con A to a gold surface results in the denaturation of the lectin. Con A is known to have hydrophobic character , and, as such, has the ability to adsorb nonspecifically to hydrophobic surfaces . Therefore, the adsorption of Con A to a gold surface, which is a moderately hydrophobic substrate, was to be expected.…”

Section: Resultsmentioning

confidence: 99%

“…Con A is known to have hydrophobic character , and, as such, has the ability to adsorb nonspecifically to hydrophobic surfaces . Therefore, the adsorption of Con A to a gold surface, which is a moderately hydrophobic substrate, was to be expected. This adsorption was confirmed using RAIRS in that the ‘amide A', ‘amide I' and ‘amide II' absorption bands used to characterize the Con A on the SAM 3 surface (Figure b) were observed when a native gold-coated substrate was exposed to a solution of the lectin.…”

Section: Resultsmentioning

confidence: 99%

“…DeBono et al 32 have previously shown, using SPR and surface plasmon microscopy (SPM), that when adsorbed directly onto a polycrystalline gold surface, the size of Con A does not correspond to either a monomeric, dimeric, or tetrameric form. This result suggests that direct adsorption of Con A to a gold surface results in the denaturation of the lectin.…”

Section: Rairs Characterization Of the Interaction Between A Sam Of 3...mentioning

confidence: 99%

See 1 more Smart Citation

Self-Assembled Carbohydrate Monolayers: Formation and Surface Selective Molecular Recognition

et al. 1998

View full text Add to dashboard Cite

The formation of self-assembled monolayers (SAMs) of representative thiocarbohydrate derivatives onto a gold surface has been investigated to build an artificial carbohydrate scaffold to mimic non-bonded molecular recognition phenomena. Three types of carbohydrate SAMs were formulated from (i) 1-β-Dthioglucose (1), (ii) 1-β-D-thioglucose tetraacetate (2), and (iii) 2-mercaptoethyl R-D-mannopyranoside (3). Subsequently, each SAM was spectroscopically characterized by reflection-absorption infrared spectroscopy (RAIRS). Deprotection of the acylated carbohydrate SAM was achieved in situ, indicating that chemical transformation may be performed without disruption of the sulfursgold bond. With the mannose derivative, in which the carbohydrate moiety was separated from the gold surface by the spacer unit sOCH2CH2SH, it was possible to demonstrate that such a carbohydrate SAM was able to interact selectively with a specific carbohydrate binding protein, i.e., concanavalin A (Con A). Exposure of the mannose derived SAM to a solution of Con A led to a specific binding interaction as measured by RAIRS and surface plasmon resonance (SPR). In contrast, on exposure of the mannose SAM to the L-fucose-specific lectin tetragonolobus purpureas, no such binding was observed. These results suggest that highly ordered SAMs of specifically designed carbohydrate derivatives can be formulated to mimic natural cell surface structures and used to study selective molecular recognition interactions.

show abstract

“…However, nitric oxide binding to polyacrylamide entrapped cytochrome cA was found to be nonreversible, with the authors speculating that the protein was modified in the polymer matrix. Additionally, the direct attachment of a protein to a gold surface may not be the ideal method for the immobilisation of the recognition element of the biosensing system, as it has been shown that proteins denature when adsorbed directly on gold surfaces, 25,26 an effect which we have also recently observed with the protein concanavalin A. 27 Barker et al 19 also found that the cytochrome cA protein was bacterially destroyed when stored in solution for up to 2 weeks, which meant that their sensors were used within 1 week of fabrication.…”

Section: Introductionmentioning

confidence: 99%

Optical biosensing of nitric oxide using the metalloprotein cytochrome c′

Blyth¹,

Aylott²,

Russell³

et al. 1999

Analyst

View full text Add to dashboard Cite

The metalloprotein cytochrome c' was extracted and purified from the bacterium Paracoccus denitrificans in order to develop a specific biosensing system for nitric oxide (NO). The metalloprotein was encapsulated in a porous silicate sol-gel glass to enable spectroscopic changes in the haem centre as a function of NO ligation to be quantified using absorption measurements. Spectroscopic evidence suggested that, between 2 and 4 d after encapsulation, the cytochrome c' protein changed conformation in the locality of the haem moiety, possibly from a five to a six coordinate haem centre. Such conformational changes were also observed when the cytochrome c' was stored in solution, although over a 2-3 month period. The conformational changes occurring in the protein altered the spectral characteristics of the reduced, oxidised and nitrosyl complex of the cytochrome c' and appear to change the binding affinity of the protein towards NO. However, the encapsulated (reconformed) cytochrome c' was shown to retain its selectivity towards NO with good reproducibility (seven consecutive measurements of NO produced an intensity value with a relative standard deviation of 0.28%). An NO calibration curve, using the in situ release of NO from the donor diethylamine NONOate, was obtained for the encapsulated cytochrome c' with an approximate working range of 10-400 mumol l-1.

show abstract

Concanavalin A and Polysaccharide on Gold Surfaces

Cited by 5 publications

References 0 publications

Comparative Study of the Binding of Concanavalin A to Self-Assembled Monolayers Containing a Thiolated α-Mannoside on Flat Gold and on Nanoporous Gold

Comparative Study of the Binding of Concanavalin A to Self-Assembled Monolayers Containing a Thiolated α-Mannoside on Flat Gold and on Nanoporous Gold

Self-Assembled Carbohydrate Monolayers: Formation and Surface Selective Molecular Recognition

Optical biosensing of nitric oxide using the metalloprotein cytochrome c′

Contact Info

Product

Resources

About