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Generic Structures of Cytotoxic Liprotides: Nano‐Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins
Author(s) -
Kaspersen Jørn D.,
Pedersen Jannik N.,
Hansted Jon G.,
Nielsen Søren B.,
Sakthivel Srinivasan,
Wilhelm Kristina,
Nemashkalova Ekaterina L.,
Permyakov Sergei E.,
Permyakov Eugene A.,
Pinto Oliveira Cristiano Luis,
MorozovaRoche Ludmilla A.,
Otzen Daniel E.,
Pedersen Jan Skov
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402407
Subject(s) - oleic acid , small angle x ray scattering , chemistry , micelle , peptide , cytotoxic t cell , shell (structure) , crystallography , biophysics , biochemistry , materials science , scattering , organic chemistry , biology , physics , aqueous solution , optics , in vitro , composite material
The cytotoxic complex formed between α‐lactalbumin and oleic acid (OA) has inspired many studies on protein–fatty acid complexes, but structural insight remains sparse. After having used small‐angle X‐ray scattering (SAXS) to obtain structural information, we present a new, generic structural model of cytotoxic protein–oleic acid complexes, which we have termed liprotides (lipids and partially denatured proteins). Twelve liprotides formed from seven structurally unrelated proteins and prepared by different procedures all displayed core–shell structures, each with a micellar OA core and a shell consisting of flexible, partially unfolded protein, which stabilizes the OA micelle. The common structure explains similar effects exerted on cells by different liprotides and is consistent with a cargo off‐loading of the OA into cell membranes.