Protein antigen adsorption to the DDA/TDB liposomal adjuvant: effect on protein structure, stability, and liposome physicochemical characteristics

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Protein antigen adsorption to the DDA/TDB liposomal adjuvant : effect on protein structure, stability, and liposome physicochemical characteristics. / Hamborg, Mette ; Jorgensen, Lene; Bojsen, Anders Riber; Christensen, Dennis; Foged, Camilla.

In: Pharmaceutical Research, Vol. 30, No. 1, 2013, p. 140-55.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hamborg, M, Jorgensen, L, Bojsen, AR, Christensen, D & Foged, C 2013, 'Protein antigen adsorption to the DDA/TDB liposomal adjuvant: effect on protein structure, stability, and liposome physicochemical characteristics', Pharmaceutical Research, vol. 30, no. 1, pp. 140-55. https://doi.org/10.1007/s11095-012-0856-8

APA

Hamborg, M., Jorgensen, L., Bojsen, A. R., Christensen, D., & Foged, C. (2013). Protein antigen adsorption to the DDA/TDB liposomal adjuvant: effect on protein structure, stability, and liposome physicochemical characteristics. Pharmaceutical Research, 30(1), 140-55. https://doi.org/10.1007/s11095-012-0856-8

Vancouver

Hamborg M, Jorgensen L, Bojsen AR, Christensen D, Foged C. Protein antigen adsorption to the DDA/TDB liposomal adjuvant: effect on protein structure, stability, and liposome physicochemical characteristics. Pharmaceutical Research. 2013;30(1):140-55. https://doi.org/10.1007/s11095-012-0856-8

Author

Hamborg, Mette ; Jorgensen, Lene ; Bojsen, Anders Riber ; Christensen, Dennis ; Foged, Camilla. / Protein antigen adsorption to the DDA/TDB liposomal adjuvant : effect on protein structure, stability, and liposome physicochemical characteristics. In: Pharmaceutical Research. 2013 ; Vol. 30, No. 1. pp. 140-55.

Bibtex

@article{f285766219b345c29567e78d9c1f239c,
title = "Protein antigen adsorption to the DDA/TDB liposomal adjuvant: effect on protein structure, stability, and liposome physicochemical characteristics",
abstract = "Understanding the nature of adjuvant-antigen interactions is important for the future design of efficient and safe subunit vaccines, but remains an analytical challenge. We studied the interactions between three model protein antigens and the clinically tested cationic liposomal adjuvant composed of dimethyldioctadecylammonium (DDA) and trehalose 6,6'-dibehenate (TDB).",
author = "Mette Hamborg and Lene Jorgensen and Bojsen, {Anders Riber} and Dennis Christensen and Camilla Foged",
year = "2013",
doi = "10.1007/s11095-012-0856-8",
language = "English",
volume = "30",
pages = "140--55",
journal = "Pharmaceutical Research",
issn = "0724-8741",
publisher = "Springer",
number = "1",

}

RIS

TY - JOUR

T1 - Protein antigen adsorption to the DDA/TDB liposomal adjuvant

T2 - effect on protein structure, stability, and liposome physicochemical characteristics

AU - Hamborg, Mette

AU - Jorgensen, Lene

AU - Bojsen, Anders Riber

AU - Christensen, Dennis

AU - Foged, Camilla

PY - 2013

Y1 - 2013

N2 - Understanding the nature of adjuvant-antigen interactions is important for the future design of efficient and safe subunit vaccines, but remains an analytical challenge. We studied the interactions between three model protein antigens and the clinically tested cationic liposomal adjuvant composed of dimethyldioctadecylammonium (DDA) and trehalose 6,6'-dibehenate (TDB).

AB - Understanding the nature of adjuvant-antigen interactions is important for the future design of efficient and safe subunit vaccines, but remains an analytical challenge. We studied the interactions between three model protein antigens and the clinically tested cationic liposomal adjuvant composed of dimethyldioctadecylammonium (DDA) and trehalose 6,6'-dibehenate (TDB).

U2 - 10.1007/s11095-012-0856-8

DO - 10.1007/s11095-012-0856-8

M3 - Journal article

C2 - 22956169

VL - 30

SP - 140

EP - 155

JO - Pharmaceutical Research

JF - Pharmaceutical Research

SN - 0724-8741

IS - 1

ER -

ID: 43971760