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dc.contributor.authorZalygin, Aen_NZ
dc.contributor.authorSolovyeva, Den_NZ
dc.contributor.authorVaskan, Ien_NZ
dc.contributor.authorHenry, Sen_NZ
dc.contributor.authorSchaefer, Men_NZ
dc.contributor.authorVolynsky, Pen_NZ
dc.contributor.authorTuzikov, Aen_NZ
dc.contributor.authorKorchagina, Een_NZ
dc.contributor.authorRyzhov, Ien_NZ
dc.contributor.authorNizovtsev, Aen_NZ
dc.contributor.authorMochalov, Ken_NZ
dc.contributor.authorEfremov, Ren_NZ
dc.contributor.authorShtykova, Een_NZ
dc.contributor.authorOleinikov, Ven_NZ
dc.contributor.authorBovin, Nen_NZ
dc.date.accessioned2020-04-08T04:36:26Z
dc.date.available2020-04-08T04:36:26Z
dc.identifier.citationChemistryOpen. doi:10.1002/open.201900276
dc.identifier.issn2191-1363en_NZ
dc.identifier.urihttp://hdl.handle.net/10292/13257
dc.description.abstractThe synthetic function‐spacer‐lipid (FSL) amphiphile biotin‐CMG‐DOPE is widely used for delicate ligation of living cells with biotin residues under physiological conditions. Since this molecule has an “apolar‐polar‐hydrophobic” gemini structure, the supramolecular organization is expected to differ significantly from the classical micelle. Its organization is investigated with experimental methods and molecular dynamics simulations (MDS). Although the linear length of a single biotin‐CMG‐DOPE molecule is 9.5 nm, the size of the dominant supramer globule is only 14.6 nm. Investigations found that while the DOPE tails form a hydrophobic core, the polar CMG spacer folds back upon itself and predominantly places the biotin reside inside the globule or planar layer. MDS demonstrates that <10 % of biotin residues on the highly water dispersible globules and only 1 % of biotin residues in layer coatings are in an linear conformation and exposing biotin into the aqueous medium. This explains why in biotin‐CMG‐DOPE apolar biotin residues both in water dispersible globules and coatings on solid surfaces are still capable of interacting with streptavidin.
dc.languageenen_NZ
dc.publisherWileyen_NZ
dc.relation.urihttps://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/open.201900276
dc.rights© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
dc.subjectAmphiphiles; Function-spacer-lipid; Biotin; Molecular dynamics; Supramers; Molecular dynamics simulations
dc.titleStructure of Supramers Formed by the Amphiphile Biotin-CMG-DOPEen_NZ
dc.typeJournal Article
dc.rights.accessrightsOpenAccessen_NZ
dc.identifier.doi10.1002/open.201900276en_NZ
pubs.elements-id373734
aut.relation.journalChemistryOpenen_NZ


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