Aarhus University Seal

Daniel Otzen

Structures and mechanisms of formation of liprotides

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

Standard

Structures and mechanisms of formation of liprotides. / Pedersen, Jannik Nedergaard; Frislev, Henriette Kristina Søster; Pedersen, Jan Skov et al.

In: B B A - Proteins and Proteomics, Vol. 1868, No. 11, 140505, 11.2020.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

Harvard

Pedersen, JN, Frislev, HKS, Pedersen, JS & Otzen, D 2020, 'Structures and mechanisms of formation of liprotides', B B A - Proteins and Proteomics, vol. 1868, no. 11, 140505. https://doi.org/10.1016/j.bbapap.2020.140505

APA

Pedersen, J. N., Frislev, H. K. S., Pedersen, J. S., & Otzen, D. (2020). Structures and mechanisms of formation of liprotides. B B A - Proteins and Proteomics, 1868(11), [140505]. https://doi.org/10.1016/j.bbapap.2020.140505

CBE

Pedersen JN, Frislev HKS, Pedersen JS, Otzen D. 2020. Structures and mechanisms of formation of liprotides. B B A - Proteins and Proteomics. 1868(11):Article 140505. https://doi.org/10.1016/j.bbapap.2020.140505

MLA

Pedersen, Jannik Nedergaard et al. "Structures and mechanisms of formation of liprotides". B B A - Proteins and Proteomics. 2020. 1868(11). https://doi.org/10.1016/j.bbapap.2020.140505

Vancouver

Pedersen JN, Frislev HKS, Pedersen JS, Otzen D. Structures and mechanisms of formation of liprotides. B B A - Proteins and Proteomics. 2020 Nov;1868(11):140505. doi: 10.1016/j.bbapap.2020.140505

Author

Pedersen, Jannik Nedergaard ; Frislev, Henriette Kristina Søster ; Pedersen, Jan Skov et al. / Structures and mechanisms of formation of liprotides. In: B B A - Proteins and Proteomics. 2020 ; Vol. 1868, No. 11.

Bibtex

@article{86e1e8ccb3044eebbed03ae1c8d45d2d,
title = "Structures and mechanisms of formation of liprotides",
abstract = "Many proteins form complexes called liprotides with oleic acid and other cis-fatty acids under conditions where the protein is partially unfolded. The complexes vary in structure depending on the ratio of protein and lipid, but the most common structural organization is the core-shell structure, in which a layer of dynamic, partially unfolded and extended proteins surrounds a micelle-like fatty acid core. This structure, first reported for α-lactalbumin together with OA, resembles complexes formed between proteins and anionic surfactants like SDS. Liprotides first rose to fame through their anti-carcinogenic properties which still remains promising for topical applications though not yet implemented in the clinic. In addition, liprotides show potential in drug delivery thanks to the ability of the micelle core to solubilize and stabilize hydrophobic compounds, though applications are challenged by their sensitivity to acidic pH and dynamic exchange of lipids which makes them easy prey for serum {"}hoovers{"} such as albumin. However, liprotides are also of fundamental interest as a generic {"}protein complex structure{"}, demonstrating the many and varied structural consequences of protein-lipid interactions. Here we provide an overview of the different types of liprotide complexes, ranging from quasi-native complexes via core-shell structures to multi-layer structures, and discuss the many conditions under which they form. Given the many variable types of complexes that can form, rigorous biophysical analysis (stoichiometry, shape and structure of the complexes) remains crucial for a complete understanding of the mechanisms of action of this fascinating group of protein-lipid complexes both in vitro and in vivo.",
author = "Pedersen, {Jannik Nedergaard} and Frislev, {Henriette Kristina S{\o}ster} and Pedersen, {Jan Skov} and Daniel Otzen",
note = "Copyright {\textcopyright} 2020 Elsevier B.V. All rights reserved.",
year = "2020",
month = nov,
doi = "10.1016/j.bbapap.2020.140505",
language = "English",
volume = "1868",
journal = "B B A - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier BV",
number = "11",

}

RIS

TY - JOUR

T1 - Structures and mechanisms of formation of liprotides

AU - Pedersen, Jannik Nedergaard

AU - Frislev, Henriette Kristina Søster

AU - Pedersen, Jan Skov

AU - Otzen, Daniel

N1 - Copyright © 2020 Elsevier B.V. All rights reserved.

PY - 2020/11

Y1 - 2020/11

N2 - Many proteins form complexes called liprotides with oleic acid and other cis-fatty acids under conditions where the protein is partially unfolded. The complexes vary in structure depending on the ratio of protein and lipid, but the most common structural organization is the core-shell structure, in which a layer of dynamic, partially unfolded and extended proteins surrounds a micelle-like fatty acid core. This structure, first reported for α-lactalbumin together with OA, resembles complexes formed between proteins and anionic surfactants like SDS. Liprotides first rose to fame through their anti-carcinogenic properties which still remains promising for topical applications though not yet implemented in the clinic. In addition, liprotides show potential in drug delivery thanks to the ability of the micelle core to solubilize and stabilize hydrophobic compounds, though applications are challenged by their sensitivity to acidic pH and dynamic exchange of lipids which makes them easy prey for serum "hoovers" such as albumin. However, liprotides are also of fundamental interest as a generic "protein complex structure", demonstrating the many and varied structural consequences of protein-lipid interactions. Here we provide an overview of the different types of liprotide complexes, ranging from quasi-native complexes via core-shell structures to multi-layer structures, and discuss the many conditions under which they form. Given the many variable types of complexes that can form, rigorous biophysical analysis (stoichiometry, shape and structure of the complexes) remains crucial for a complete understanding of the mechanisms of action of this fascinating group of protein-lipid complexes both in vitro and in vivo.

AB - Many proteins form complexes called liprotides with oleic acid and other cis-fatty acids under conditions where the protein is partially unfolded. The complexes vary in structure depending on the ratio of protein and lipid, but the most common structural organization is the core-shell structure, in which a layer of dynamic, partially unfolded and extended proteins surrounds a micelle-like fatty acid core. This structure, first reported for α-lactalbumin together with OA, resembles complexes formed between proteins and anionic surfactants like SDS. Liprotides first rose to fame through their anti-carcinogenic properties which still remains promising for topical applications though not yet implemented in the clinic. In addition, liprotides show potential in drug delivery thanks to the ability of the micelle core to solubilize and stabilize hydrophobic compounds, though applications are challenged by their sensitivity to acidic pH and dynamic exchange of lipids which makes them easy prey for serum "hoovers" such as albumin. However, liprotides are also of fundamental interest as a generic "protein complex structure", demonstrating the many and varied structural consequences of protein-lipid interactions. Here we provide an overview of the different types of liprotide complexes, ranging from quasi-native complexes via core-shell structures to multi-layer structures, and discuss the many conditions under which they form. Given the many variable types of complexes that can form, rigorous biophysical analysis (stoichiometry, shape and structure of the complexes) remains crucial for a complete understanding of the mechanisms of action of this fascinating group of protein-lipid complexes both in vitro and in vivo.

U2 - 10.1016/j.bbapap.2020.140505

DO - 10.1016/j.bbapap.2020.140505

M3 - Review

C2 - 32721568

VL - 1868

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

SN - 1570-9639

IS - 11

M1 - 140505

ER -