Effect of reductive methylation on the adsorption of hen lysozyme

Chen, J; Dong, Dengpan; Andrade, Joseph D.

doi:10.1016/0021-9797(82)90212-0

Cited by 13 publications

(6 citation statements)

References 9 publications

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“…However this result was unexpected because (i) changes due to methylation are smallsthe protein contains only six lysine residues, all of which are exposed on the surface, and a maximum of two methyl groups can be added per lysinesin which case only a slight change in adsorption would be expected and (ii) methylation could enhance the hydrophobicity of the protein; 11 thus, a small increase in adsorption was expected instead. Moreover our result is in contrast with those of Chen et al 6 on the adsorption of lysozyme on both hydrophilic (ultraclean) and hydrophobic (silanized) borosilicate glass: They showed that, for similar conditions in pH and ionic strength, methylated lysozyme is adsorbing preferentially to the pure one in both cases.…”

Section: Resultscontrasting

confidence: 99%

“…The only effect of the methylation is that it reduces the amount of adsorbed protein by a significant amount (about 14%). Our results are also compared with pressure−area isotherm data obtained by other authors, with adsorption of bovine serum albumin (BSA) at the air−water interface and with adsorption data of pure and methylated lysozyme on glass substrates …”

Section: Introductionmentioning

confidence: 72%

“…1,2 Labeling techniques, using either radioactive or fluorescent markers, are widely used to study the dynamics of the adsorption process. [3][4][5] It has been shown in a number of cases that these techniques do not alter the biological properties of the protein; 6 however, the influence of labeling on the adsorption behavior itself has not been studied systematically using a direct measurement method.…”

Section: Introductionmentioning

confidence: 99%

“…Our results are also compared with pressure-area isotherm data obtained by other authors, 2 with adsorption of bovine serum albumin (BSA) at the air-water interface 11 and with adsorption data of pure and methylated lysozyme on glass substrates. 6…”

Section: Introductionmentioning

confidence: 99%

“…Adsorption of proteins at interfaces plays an important role in several biological and technological processes, and a large number of studies have already been devoted to this subject. , Labeling techniques, using either radioactive or fluorescent markers, are widely used to study the dynamics of the adsorption process. − It has been shown in a number of cases that these techniques do not alter the biological properties of the protein; however, the influence of labeling on the adsorption behavior itself has not been studied systematically using a direct measurement method.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Adsorption of Lysozyme and Methylated Lysozyme at the Air−Water Interface: An X-ray Reflectivity Study

Postel¹,

Abillon²

1998

Langmuir

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Section: Resultscontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 72%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Adsorption of Lysozyme and Methylated Lysozyme at the Air−Water Interface: An X-ray Reflectivity Study

Postel¹,

Abillon²

1998

Langmuir

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The adsorption of lysozymes: A model system

Hansen

Ely

Horsley

et al. 1988

Makromolekulare Chemie. Macromolecular Symposia

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Hen egg white lysozyme was adsorbed onto clean borosilicate glass and n‐pentyl silane‐treated glass surfaces. Both modified (reductively methylated) and native lysozyme were studied. Variable angle X‐ray photoelectron spectroscopy (VA‐XPS) suggested differences in the nature of the adsorbed layer depending on substrate properties, as well as on degree of methylation of the protein. Adsorbed film thickness (as measured in the dehydrated state by XPS) ranged from 14 Å on hydrophilic glass to 25 Å on the hydrophobic surface. Degree of surface coverage ranged from 45% on the hydrophobic to 69% on the hydrophilic surface. The results suggest that lysozyme unfolds to a greater extent and covers more surface on the hydrophilic glass, possibly due to strong electrostatic interactions at the pH 7.4 conditions used in the study. An analysis of the surface structure of native hen lysozyme by molecular graphics has also been performed, suggesting that adsorption on hydrophobic surfaces should occur via the hydrophobic patch opposite the enzyme active site cleft. A comparison with human lysozyme has also been made using total internal reflection fluorescence (TIRF) spectroscopy to measure protein adsorption on model surfaces. The two proteins have significantly different interfacial properties.

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