Publication

Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates

Mensink, M. A., S ̌ib í k, J., Frijlink, H. W., Maarschalk, K. V. D. V., Hinrichs, W. L. J. & Zeitler, J. A., Oct-2017, In : Molecular pharmaceutics. 14, 10, p. 3550-3557 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Mensink, M. A., S ̌ib í k, J., Frijlink, H. W., Maarschalk, K. V. D. V., Hinrichs, W. L. J., & Zeitler, J. A. (2017). Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates. Molecular pharmaceutics, 14(10), 3550-3557. https://doi.org/10.1021/acs.molpharmaceut.7b00568

Author

Mensink, M. A. ; S ̌ib í k, J. ; Frijlink, H. W. ; Maarschalk, K. van der Voort ; Hinrichs, W. L. J. ; Zeitler, J. A. / Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates. In: Molecular pharmaceutics. 2017 ; Vol. 14, No. 10. pp. 3550-3557.

Harvard

Mensink, MA, S ̌ib í k, J, Frijlink, HW, Maarschalk, KVDV, Hinrichs, WLJ & Zeitler, JA 2017, 'Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates', Molecular pharmaceutics, vol. 14, no. 10, pp. 3550-3557. https://doi.org/10.1021/acs.molpharmaceut.7b00568

Standard

Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates. / Mensink, M. A.; S ̌ib í k, J.; Frijlink, H. W.; Maarschalk, K. van der Voort; Hinrichs, W. L. J.; Zeitler, J. A.

In: Molecular pharmaceutics, Vol. 14, No. 10, 10.2017, p. 3550-3557.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Mensink MA, S ̌ib í k J, Frijlink HW, Maarschalk KVDV, Hinrichs WLJ, Zeitler JA. Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates. Molecular pharmaceutics. 2017 Oct;14(10):3550-3557. https://doi.org/10.1021/acs.molpharmaceut.7b00568


BibTeX

@article{94c5d201a71946f2b63dcc29049e56d1,
title = "Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates",
abstract = "Protein drugs play an important role in modern day medicine. Typically, these proteins are formulated as liquids requiring cold chain processing. To circumvent the cold chain and achieve better storage stability, these proteins can be dried in the presence of carbohydrates. We demonstrate that thermal gradient mid- and far-infrared spectroscopy (FTIR and THz-TDS, respectively) can provide useful information about solid-state protein carbohydrate formulations regarding mobility and intermolecular interactions. A model protein (BSA) was lyophilized in the presence of three carbohydrates with different size and protein stabilizing capacity. A gradual increase in mobility was observed with increasing temperature in formulations containing protein and/or larger carbohydrates (oligo- or polysaccharides), lacking a clear onset of fast mobility as was observed for smaller molecules. Furthermore, both techniques are able to identify the glass transition temperatures (T-g) of the samples. FTIR provides additional information as it can independently monitor changes in protein and carbohydrate bands at the T-g. Lastly, THz-TDS confirms previous findings that protein-carbohydrate interactions decrease with increasing molecular weight of the carbohydrate, which results in decreased protein stabilization.",
keywords = "terahertz time-domain spectroscopy (THz-TDS), Fourier transform infrared spectroscopy (FTIR), hydrogen bonding, molecular mobility, solid state, TERAHERTZ TIME-DOMAIN, STORAGE STABILITY, GLASSY STATE, SOLID-STATE, DYNAMICS, SUGAR, PHARMACEUTICALS, STABILIZATION, RELAXATION, MECHANISMS",
author = "Mensink, {M. A.} and {S ̌ib {\'i} k}, J. and Frijlink, {H. W.} and Maarschalk, {K. van der Voort} and Hinrichs, {W. L. J.} and Zeitler, {J. A.}",
year = "2017",
month = "10",
doi = "10.1021/acs.molpharmaceut.7b00568",
language = "English",
volume = "14",
pages = "3550--3557",
journal = "Molecular pharmaceutics",
issn = "1543-8384",
publisher = "AMER CHEMICAL SOC INC",
number = "10",

}

RIS

TY - JOUR

T1 - Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates

AU - Mensink, M. A.

AU - S ̌ib í k, J.

AU - Frijlink, H. W.

AU - Maarschalk, K. van der Voort

AU - Hinrichs, W. L. J.

AU - Zeitler, J. A.

PY - 2017/10

Y1 - 2017/10

N2 - Protein drugs play an important role in modern day medicine. Typically, these proteins are formulated as liquids requiring cold chain processing. To circumvent the cold chain and achieve better storage stability, these proteins can be dried in the presence of carbohydrates. We demonstrate that thermal gradient mid- and far-infrared spectroscopy (FTIR and THz-TDS, respectively) can provide useful information about solid-state protein carbohydrate formulations regarding mobility and intermolecular interactions. A model protein (BSA) was lyophilized in the presence of three carbohydrates with different size and protein stabilizing capacity. A gradual increase in mobility was observed with increasing temperature in formulations containing protein and/or larger carbohydrates (oligo- or polysaccharides), lacking a clear onset of fast mobility as was observed for smaller molecules. Furthermore, both techniques are able to identify the glass transition temperatures (T-g) of the samples. FTIR provides additional information as it can independently monitor changes in protein and carbohydrate bands at the T-g. Lastly, THz-TDS confirms previous findings that protein-carbohydrate interactions decrease with increasing molecular weight of the carbohydrate, which results in decreased protein stabilization.

AB - Protein drugs play an important role in modern day medicine. Typically, these proteins are formulated as liquids requiring cold chain processing. To circumvent the cold chain and achieve better storage stability, these proteins can be dried in the presence of carbohydrates. We demonstrate that thermal gradient mid- and far-infrared spectroscopy (FTIR and THz-TDS, respectively) can provide useful information about solid-state protein carbohydrate formulations regarding mobility and intermolecular interactions. A model protein (BSA) was lyophilized in the presence of three carbohydrates with different size and protein stabilizing capacity. A gradual increase in mobility was observed with increasing temperature in formulations containing protein and/or larger carbohydrates (oligo- or polysaccharides), lacking a clear onset of fast mobility as was observed for smaller molecules. Furthermore, both techniques are able to identify the glass transition temperatures (T-g) of the samples. FTIR provides additional information as it can independently monitor changes in protein and carbohydrate bands at the T-g. Lastly, THz-TDS confirms previous findings that protein-carbohydrate interactions decrease with increasing molecular weight of the carbohydrate, which results in decreased protein stabilization.

KW - terahertz time-domain spectroscopy (THz-TDS)

KW - Fourier transform infrared spectroscopy (FTIR)

KW - hydrogen bonding

KW - molecular mobility

KW - solid state

KW - TERAHERTZ TIME-DOMAIN

KW - STORAGE STABILITY

KW - GLASSY STATE

KW - SOLID-STATE

KW - DYNAMICS

KW - SUGAR

KW - PHARMACEUTICALS

KW - STABILIZATION

KW - RELAXATION

KW - MECHANISMS

U2 - 10.1021/acs.molpharmaceut.7b00568

DO - 10.1021/acs.molpharmaceut.7b00568

M3 - Article

VL - 14

SP - 3550

EP - 3557

JO - Molecular pharmaceutics

JF - Molecular pharmaceutics

SN - 1543-8384

IS - 10

ER -

ID: 49269309