Tryptophan, tryptophan-leucine, and BSA adsorption at an oil-water interface

D. Beaglehole; F. Lawson; G. Harper; M. Hossain

doi:10.1006/jcis.1997.4948

Tryptophan, tryptophan-leucine, and BSA adsorption at an oil-water interface

D. Beaglehole, F. Lawson, G. Harper, M. Hossain

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

11 Citations (Scopus)

Abstract

Adsorption of the amino acid tryptophan, the peptide tryptophan-leucine and the protein bovine serum albumin (BSA) at buffered water-oleyl alcohol interfaces has been studied by ellipsometry. Tryptophan-leucine solutions showed a systematic change in ellipticity with concentration indicating an adsorption of 0.5 mg/m² for a solution concentration of 1 g/L and evidence of saturation at that concentration. BSA showed an adsorption of 0.45 mg/m² for a concentration of 3.5 g/L with no sign of saturation, There appeared to be little adsorption of tryptophan at the interface.

Original language	English
Pages (from-to)	266-268
Number of pages	3
Journal	Journal of Colloid and Interface Science
Volume	192
Issue number	1
DOIs	https://doi.org/10.1006/jcis.1997.4948
Publication status	Published - Aug 1 1997
Externally published	Yes

ASJC Scopus subject areas

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

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abstract = "Adsorption of the amino acid tryptophan, the peptide tryptophan-leucine and the protein bovine serum albumin (BSA) at buffered water-oleyl alcohol interfaces has been studied by ellipsometry. Tryptophan-leucine solutions showed a systematic change in ellipticity with concentration indicating an adsorption of 0.5 mg/m2 for a solution concentration of 1 g/L and evidence of saturation at that concentration. BSA showed an adsorption of 0.45 mg/m2 for a concentration of 3.5 g/L with no sign of saturation, There appeared to be little adsorption of tryptophan at the interface.",

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AU - Beaglehole, D.

AU - Lawson, F.

AU - Harper, G.

AU - Hossain, M.

PY - 1997/8/1

Y1 - 1997/8/1

N2 - Adsorption of the amino acid tryptophan, the peptide tryptophan-leucine and the protein bovine serum albumin (BSA) at buffered water-oleyl alcohol interfaces has been studied by ellipsometry. Tryptophan-leucine solutions showed a systematic change in ellipticity with concentration indicating an adsorption of 0.5 mg/m2 for a solution concentration of 1 g/L and evidence of saturation at that concentration. BSA showed an adsorption of 0.45 mg/m2 for a concentration of 3.5 g/L with no sign of saturation, There appeared to be little adsorption of tryptophan at the interface.

AB - Adsorption of the amino acid tryptophan, the peptide tryptophan-leucine and the protein bovine serum albumin (BSA) at buffered water-oleyl alcohol interfaces has been studied by ellipsometry. Tryptophan-leucine solutions showed a systematic change in ellipticity with concentration indicating an adsorption of 0.5 mg/m2 for a solution concentration of 1 g/L and evidence of saturation at that concentration. BSA showed an adsorption of 0.45 mg/m2 for a concentration of 3.5 g/L with no sign of saturation, There appeared to be little adsorption of tryptophan at the interface.

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Tryptophan, tryptophan-leucine, and BSA adsorption at an oil-water interface

Abstract

ASJC Scopus subject areas

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