Probing structural changes of proteins incorporated into water-in-oil emulsions

Research output: Contribution to journalJournal articleResearchpeer-review

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Probing structural changes of proteins incorporated into water-in-oil emulsions. / Jorgensen, Lene; van de Weert, Marco; Vermehren, Charlotte; Bjerregaard, Simon; Frokjaer, Sven.

In: Journal of Pharmaceutical Sciences, Vol. 93, No. 7, 07.2004, p. 1847-59.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Jorgensen, L, van de Weert, M, Vermehren, C, Bjerregaard, S & Frokjaer, S 2004, 'Probing structural changes of proteins incorporated into water-in-oil emulsions', Journal of Pharmaceutical Sciences, vol. 93, no. 7, pp. 1847-59. https://doi.org/10.1002/jps.20097

APA

Jorgensen, L., van de Weert, M., Vermehren, C., Bjerregaard, S., & Frokjaer, S. (2004). Probing structural changes of proteins incorporated into water-in-oil emulsions. Journal of Pharmaceutical Sciences, 93(7), 1847-59. https://doi.org/10.1002/jps.20097

Vancouver

Jorgensen L, van de Weert M, Vermehren C, Bjerregaard S, Frokjaer S. Probing structural changes of proteins incorporated into water-in-oil emulsions. Journal of Pharmaceutical Sciences. 2004 Jul;93(7):1847-59. https://doi.org/10.1002/jps.20097

Author

Jorgensen, Lene ; van de Weert, Marco ; Vermehren, Charlotte ; Bjerregaard, Simon ; Frokjaer, Sven. / Probing structural changes of proteins incorporated into water-in-oil emulsions. In: Journal of Pharmaceutical Sciences. 2004 ; Vol. 93, No. 7. pp. 1847-59.

Bibtex

@article{2fcb6689d1ab49bf90217525ea0ec2fb,
title = "Probing structural changes of proteins incorporated into water-in-oil emulsions",
abstract = "The applicability of different techniques, that is, Differential Scanning Calorimetry (DSC), Fourier Transform Infrared Spectroscopy (FTIR), and intrinsic tryptophan fluorescence, for probing the structural changes of proteins in the water-in-oil emulsions are investigated using nondefatted bovine (BSA) and human serum albumin (HSA) as model proteins. FTIR shows that the overall secondary structure of the proteins changes to some extent, 12{\%} for BSA and 9{\%} for HSA, when these are incorporated into the emulsion. There was no evidence of changes in the distribution of secondary structural elements apart from the changes in overall secondary structure. A blue shift of 12 to 14 nm in the fluorescence emission maximum was observed for proteins in the emulsion and 3 to 11 nm in the simulated interior of the aqueous phase, thus indicating structural changes around the tryptophan residues. DSC scans indicated that the domains in the proteins change because the shape of the transition peaks changes, when the proteins were incorporated into the emulsions. The total enthalpy decreases for BSA and HSA when these are incorporated into the emulsion, and some changes to the transition temperatures are observed. All the applied techniques supplement each other to give a more complete picture of the structural changes in proteins in intact water-in-oil emulsions.",
keywords = "Animals, Calorimetry, Differential Scanning, Cattle, Emulsions, Humans, Oils, Protein Structure, Secondary, Serum Albumin, Water",
author = "Lene Jorgensen and {van de Weert}, Marco and Charlotte Vermehren and Simon Bjerregaard and Sven Frokjaer",
note = "Copyright 2004 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:1847-1859, 2004",
year = "2004",
month = "7",
doi = "10.1002/jps.20097",
language = "English",
volume = "93",
pages = "1847--59",
journal = "Journal of Pharmaceutical Sciences",
issn = "0022-3549",
publisher = "Elsevier",
number = "7",

}

RIS

TY - JOUR

T1 - Probing structural changes of proteins incorporated into water-in-oil emulsions

AU - Jorgensen, Lene

AU - van de Weert, Marco

AU - Vermehren, Charlotte

AU - Bjerregaard, Simon

AU - Frokjaer, Sven

N1 - Copyright 2004 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 93:1847-1859, 2004

PY - 2004/7

Y1 - 2004/7

N2 - The applicability of different techniques, that is, Differential Scanning Calorimetry (DSC), Fourier Transform Infrared Spectroscopy (FTIR), and intrinsic tryptophan fluorescence, for probing the structural changes of proteins in the water-in-oil emulsions are investigated using nondefatted bovine (BSA) and human serum albumin (HSA) as model proteins. FTIR shows that the overall secondary structure of the proteins changes to some extent, 12% for BSA and 9% for HSA, when these are incorporated into the emulsion. There was no evidence of changes in the distribution of secondary structural elements apart from the changes in overall secondary structure. A blue shift of 12 to 14 nm in the fluorescence emission maximum was observed for proteins in the emulsion and 3 to 11 nm in the simulated interior of the aqueous phase, thus indicating structural changes around the tryptophan residues. DSC scans indicated that the domains in the proteins change because the shape of the transition peaks changes, when the proteins were incorporated into the emulsions. The total enthalpy decreases for BSA and HSA when these are incorporated into the emulsion, and some changes to the transition temperatures are observed. All the applied techniques supplement each other to give a more complete picture of the structural changes in proteins in intact water-in-oil emulsions.

AB - The applicability of different techniques, that is, Differential Scanning Calorimetry (DSC), Fourier Transform Infrared Spectroscopy (FTIR), and intrinsic tryptophan fluorescence, for probing the structural changes of proteins in the water-in-oil emulsions are investigated using nondefatted bovine (BSA) and human serum albumin (HSA) as model proteins. FTIR shows that the overall secondary structure of the proteins changes to some extent, 12% for BSA and 9% for HSA, when these are incorporated into the emulsion. There was no evidence of changes in the distribution of secondary structural elements apart from the changes in overall secondary structure. A blue shift of 12 to 14 nm in the fluorescence emission maximum was observed for proteins in the emulsion and 3 to 11 nm in the simulated interior of the aqueous phase, thus indicating structural changes around the tryptophan residues. DSC scans indicated that the domains in the proteins change because the shape of the transition peaks changes, when the proteins were incorporated into the emulsions. The total enthalpy decreases for BSA and HSA when these are incorporated into the emulsion, and some changes to the transition temperatures are observed. All the applied techniques supplement each other to give a more complete picture of the structural changes in proteins in intact water-in-oil emulsions.

KW - Animals

KW - Calorimetry, Differential Scanning

KW - Cattle

KW - Emulsions

KW - Humans

KW - Oils

KW - Protein Structure, Secondary

KW - Serum Albumin

KW - Water

U2 - 10.1002/jps.20097

DO - 10.1002/jps.20097

M3 - Journal article

C2 - 15176072

VL - 93

SP - 1847

EP - 1859

JO - Journal of Pharmaceutical Sciences

JF - Journal of Pharmaceutical Sciences

SN - 0022-3549

IS - 7

ER -

ID: 44640658