Characteristics of interfacial water affected by proteins adsorbed on activated carbon

T. A. Alexeeva; N. I. Lebovka; V. M. Gun'ko; V. V. Strashko; S. V. Mikhalovsky

doi:10.1016/j.jcis.2004.06.030

Characteristics of interfacial water affected by proteins adsorbed on activated carbon

T. A. Alexeeva, N. I. Lebovka, V. M. Gun'ko, V. V. Strashko, S. V. Mikhalovsky

School of Engineering and Digital Sciences

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

The influence of proteins (bovine serum albumin, BSA, and mouse γ-globulin, IgG) physically adsorbed or covalently attached via coupling with N-cyclohexyl-N′-(2-morpholinoethyl) carbodiimide methyl-p- toluenesulfonate, CMC, to the surface of activated carbon SCN (spherical carbon with nitrogen) on the mobility of interfacial water molecules was studied by means of ¹H NMR spectroscopy with freezing-out of bulk water at 180<T<273 K. Relaxation processes in the interfacial non-freezing water were investigated measuring transverse time t₂ of proton relaxation dependence on the presence of proteins and CMC. The distribution function of activation free energy of relaxation (with a maximum at 20-22 kJ/mol) was calculated for the protein-water-carbon systems using a regularization procedure and the relationships between t₂ and the amounts of the interfacial water unfrozen at T<250 K assuming the Arrhenius-type dependence for t ₂^-1 on temperature. The state of unfrozen water in pores of SCN shows that the low temperature relaxation processes occur in narrow pores with half-width X<1.5 nm.

Original language	English
Pages (from-to)	333-341
Number of pages	9
Journal	Journal of Colloid and Interface Science
Volume	278
Issue number	2
DOIs	https://doi.org/10.1016/j.jcis.2004.06.030
Publication status	Published - Oct 15 2004

Keywords

Activated carbon
H NMR spectroscopy
Microporosity
Nonfreezable interfacial water
Protein chemisorption
Protein immobilization
Surface properties

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Biomaterials
Surfaces, Coatings and Films
Colloid and Surface Chemistry

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title = "Characteristics of interfacial water affected by proteins adsorbed on activated carbon",

abstract = "The influence of proteins (bovine serum albumin, BSA, and mouse γ-globulin, IgG) physically adsorbed or covalently attached via coupling with N-cyclohexyl-N′-(2-morpholinoethyl) carbodiimide methyl-p- toluenesulfonate, CMC, to the surface of activated carbon SCN (spherical carbon with nitrogen) on the mobility of interfacial water molecules was studied by means of 1H NMR spectroscopy with freezing-out of bulk water at 180<T<273 K. Relaxation processes in the interfacial non-freezing water were investigated measuring transverse time t2 of proton relaxation dependence on the presence of proteins and CMC. The distribution function of activation free energy of relaxation (with a maximum at 20-22 kJ/mol) was calculated for the protein-water-carbon systems using a regularization procedure and the relationships between t2 and the amounts of the interfacial water unfrozen at T<250 K assuming the Arrhenius-type dependence for t 2-1 on temperature. The state of unfrozen water in pores of SCN shows that the low temperature relaxation processes occur in narrow pores with half-width X<1.5 nm.",

keywords = "Activated carbon, H NMR spectroscopy, Microporosity, Nonfreezable interfacial water, Protein chemisorption, Protein immobilization, Surface properties",

author = "Alexeeva, {T. A.} and Lebovka, {N. I.} and Gun'ko, {V. M.} and Strashko, {V. V.} and Mikhalovsky, {S. V.}",

note = "Funding Information: This work was partly supported by EPSRC (UK) Grant GR/R05154. V.M.G. thanks the Royal Society for financial support of his visit to the University of Brighton, UK. ",

year = "2004",

month = oct,

day = "15",

doi = "10.1016/j.jcis.2004.06.030",

language = "English",

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pages = "333--341",

journal = "Journal of Colloid and Interface Science",

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T1 - Characteristics of interfacial water affected by proteins adsorbed on activated carbon

AU - Alexeeva, T. A.

AU - Lebovka, N. I.

AU - Gun'ko, V. M.

AU - Strashko, V. V.

AU - Mikhalovsky, S. V.

N1 - Funding Information: This work was partly supported by EPSRC (UK) Grant GR/R05154. V.M.G. thanks the Royal Society for financial support of his visit to the University of Brighton, UK.

PY - 2004/10/15

Y1 - 2004/10/15

N2 - The influence of proteins (bovine serum albumin, BSA, and mouse γ-globulin, IgG) physically adsorbed or covalently attached via coupling with N-cyclohexyl-N′-(2-morpholinoethyl) carbodiimide methyl-p- toluenesulfonate, CMC, to the surface of activated carbon SCN (spherical carbon with nitrogen) on the mobility of interfacial water molecules was studied by means of 1H NMR spectroscopy with freezing-out of bulk water at 180<T<273 K. Relaxation processes in the interfacial non-freezing water were investigated measuring transverse time t2 of proton relaxation dependence on the presence of proteins and CMC. The distribution function of activation free energy of relaxation (with a maximum at 20-22 kJ/mol) was calculated for the protein-water-carbon systems using a regularization procedure and the relationships between t2 and the amounts of the interfacial water unfrozen at T<250 K assuming the Arrhenius-type dependence for t 2-1 on temperature. The state of unfrozen water in pores of SCN shows that the low temperature relaxation processes occur in narrow pores with half-width X<1.5 nm.

AB - The influence of proteins (bovine serum albumin, BSA, and mouse γ-globulin, IgG) physically adsorbed or covalently attached via coupling with N-cyclohexyl-N′-(2-morpholinoethyl) carbodiimide methyl-p- toluenesulfonate, CMC, to the surface of activated carbon SCN (spherical carbon with nitrogen) on the mobility of interfacial water molecules was studied by means of 1H NMR spectroscopy with freezing-out of bulk water at 180<T<273 K. Relaxation processes in the interfacial non-freezing water were investigated measuring transverse time t2 of proton relaxation dependence on the presence of proteins and CMC. The distribution function of activation free energy of relaxation (with a maximum at 20-22 kJ/mol) was calculated for the protein-water-carbon systems using a regularization procedure and the relationships between t2 and the amounts of the interfacial water unfrozen at T<250 K assuming the Arrhenius-type dependence for t 2-1 on temperature. The state of unfrozen water in pores of SCN shows that the low temperature relaxation processes occur in narrow pores with half-width X<1.5 nm.

KW - Activated carbon

KW - H NMR spectroscopy

KW - Microporosity

KW - Nonfreezable interfacial water

KW - Protein chemisorption

KW - Protein immobilization

KW - Surface properties

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