Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions

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Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions. / Høgstedt, Ulrich B; Schwach, Grégoire; van de Weert, Marco; Østergaard, Jesper.

In: European Journal of Pharmaceutical Sciences, Vol. 93, 25.07.2016, p. 21-28.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Høgstedt, UB, Schwach, G, van de Weert, M & Østergaard, J 2016, 'Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions', European Journal of Pharmaceutical Sciences, vol. 93, pp. 21-28. https://doi.org/10.1016/j.ejps.2016.07.015

APA

Høgstedt, U. B., Schwach, G., van de Weert, M., & Østergaard, J. (2016). Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions. European Journal of Pharmaceutical Sciences, 93, 21-28. https://doi.org/10.1016/j.ejps.2016.07.015

Vancouver

Høgstedt UB, Schwach G, van de Weert M, Østergaard J. Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions. European Journal of Pharmaceutical Sciences. 2016 Jul 25;93:21-28. https://doi.org/10.1016/j.ejps.2016.07.015

Author

Høgstedt, Ulrich B ; Schwach, Grégoire ; van de Weert, Marco ; Østergaard, Jesper. / Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions. In: European Journal of Pharmaceutical Sciences. 2016 ; Vol. 93. pp. 21-28.

Bibtex

@article{96042b0fc4c94feb84b8271a5d863474,
title = "Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions",
abstract = "Protein-protein and peptide-peptide (self-)interactions are of key importance in understanding the physiochemical behavior of proteins and peptides in solution. However, due to the small size of peptide molecules, characterization of these interactions is more challenging than for proteins. In this work, we show that protein-protein and peptide-peptide interactions can advantageously be investigated by measurement of the diffusion coefficient using Taylor Dispersion Analysis. Through comparison to Dynamic Light Scattering it was shown that Taylor Dispersion Analysis is well suited for the characterization of protein-protein interactions of solutions of α-lactalbumin and human serum albumin. The peptide-peptide interactions of three selected peptides were then investigated in a concentration range spanning from 0.5mg/ml up to 80mg/ml using Taylor Dispersion Analysis. The peptide-peptide interactions determination indicated that multibody interactions significantly affect the PPIs at concentration levels above 25mg/ml for the two charged peptides. Relative viscosity measurements, performed using the capillary based setup applied for Taylor Dispersion Analysis, showed that the viscosity of the peptide solutions increased with concentration. Our results indicate that a viscosity difference between run buffer and sample in Taylor Dispersion Analysis may result in overestimation of the measured diffusion coefficient. Thus, Taylor Dispersion Analysis provides a practical, but as yet primarily qualitative, approach to assessment of the colloidal stability of both peptide and protein formulations.",
author = "H{\o}gstedt, {Ulrich B} and Gr{\'e}goire Schwach and {van de Weert}, Marco and Jesper {\O}stergaard",
note = "Copyright {\circledC} 2016. Published by Elsevier B.V.",
year = "2016",
month = "7",
day = "25",
doi = "10.1016/j.ejps.2016.07.015",
language = "English",
volume = "93",
pages = "21--28",
journal = "European Journal of Pharmaceutical Sciences",
issn = "0928-0987",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Taylor Dispersion Analysis as a promising tool for assessment of peptide-peptide interactions

AU - Høgstedt, Ulrich B

AU - Schwach, Grégoire

AU - van de Weert, Marco

AU - Østergaard, Jesper

N1 - Copyright © 2016. Published by Elsevier B.V.

PY - 2016/7/25

Y1 - 2016/7/25

N2 - Protein-protein and peptide-peptide (self-)interactions are of key importance in understanding the physiochemical behavior of proteins and peptides in solution. However, due to the small size of peptide molecules, characterization of these interactions is more challenging than for proteins. In this work, we show that protein-protein and peptide-peptide interactions can advantageously be investigated by measurement of the diffusion coefficient using Taylor Dispersion Analysis. Through comparison to Dynamic Light Scattering it was shown that Taylor Dispersion Analysis is well suited for the characterization of protein-protein interactions of solutions of α-lactalbumin and human serum albumin. The peptide-peptide interactions of three selected peptides were then investigated in a concentration range spanning from 0.5mg/ml up to 80mg/ml using Taylor Dispersion Analysis. The peptide-peptide interactions determination indicated that multibody interactions significantly affect the PPIs at concentration levels above 25mg/ml for the two charged peptides. Relative viscosity measurements, performed using the capillary based setup applied for Taylor Dispersion Analysis, showed that the viscosity of the peptide solutions increased with concentration. Our results indicate that a viscosity difference between run buffer and sample in Taylor Dispersion Analysis may result in overestimation of the measured diffusion coefficient. Thus, Taylor Dispersion Analysis provides a practical, but as yet primarily qualitative, approach to assessment of the colloidal stability of both peptide and protein formulations.

AB - Protein-protein and peptide-peptide (self-)interactions are of key importance in understanding the physiochemical behavior of proteins and peptides in solution. However, due to the small size of peptide molecules, characterization of these interactions is more challenging than for proteins. In this work, we show that protein-protein and peptide-peptide interactions can advantageously be investigated by measurement of the diffusion coefficient using Taylor Dispersion Analysis. Through comparison to Dynamic Light Scattering it was shown that Taylor Dispersion Analysis is well suited for the characterization of protein-protein interactions of solutions of α-lactalbumin and human serum albumin. The peptide-peptide interactions of three selected peptides were then investigated in a concentration range spanning from 0.5mg/ml up to 80mg/ml using Taylor Dispersion Analysis. The peptide-peptide interactions determination indicated that multibody interactions significantly affect the PPIs at concentration levels above 25mg/ml for the two charged peptides. Relative viscosity measurements, performed using the capillary based setup applied for Taylor Dispersion Analysis, showed that the viscosity of the peptide solutions increased with concentration. Our results indicate that a viscosity difference between run buffer and sample in Taylor Dispersion Analysis may result in overestimation of the measured diffusion coefficient. Thus, Taylor Dispersion Analysis provides a practical, but as yet primarily qualitative, approach to assessment of the colloidal stability of both peptide and protein formulations.

U2 - 10.1016/j.ejps.2016.07.015

DO - 10.1016/j.ejps.2016.07.015

M3 - Journal article

C2 - 27460846

VL - 93

SP - 21

EP - 28

JO - European Journal of Pharmaceutical Sciences

JF - European Journal of Pharmaceutical Sciences

SN - 0928-0987

ER -

ID: 164467106