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Structure of Supramers Formed by the Amphiphile Biotin-CMG-DOPE |
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| Authors: | Anton Zalygin Daria Solovyeva Ivan Vaskan Dr Stephen Henry Dr Marcel Schaefer Dr Pavel Volynsky Dr Alexander Tuzikov Dr Elena Korchagina Dr Ivan Ryzhov Dr Alexey Nizovtsev Dr Konstantin Mochalov Prof Roman Efremov Dr Eleonora Shtykova Dr Vladimir Oleinikov Prof Nicolai Bovin |
| Institution: | 1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya str., Moscow, 117997 Russia;2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya str., Moscow, 117997 Russia
National Research Nuclear University MEPhI (Moscow Engineering Physics Institute), Kashirskoe shosse 31, Moscow, 115409 Russian Federation;3. School of Engineering, Computer & Mathematical Sciences, Auckland University of Technology, Auckland, 1010 New Zealand;4. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya str., Moscow, 117997 Russia National Research University Higher School of Economics, Myasnitskaya Str. 20, Moscow, 101000 Russian Federation;5. Shubnikov Institute of Crystallography of Federal Scientific Research Centre 'Crystallography and Photonics' of Russian Academy of Sciences, Moscow, 119333 Russian Federation Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, 119991 Russian Federation |
| Abstract: | The 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. |
| Keywords: | amphiphiles function-spacer-lipid biotin molecular dynamics supramers molecular dynamics simulations |