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Design of PG-Surfactants Bearing Polyacrylamide Polymer Chain to Solubilize Membrane Proteins in a Surfactant-Free Buffer.

ABSTRACT: The development of techniques capable of using membrane proteins in a surfactant-free aqueous buffer is an attractive research area, and it should be elucidated for various membrane protein studies. To this end, we examined a method using new solubilization surfactants that do not detach from membrane protein surfaces once bound. The designed solubilization surfactants, DKDKC₁₂K-PA_n (n = 5, 7, and 18), consist of two parts: one is the lipopeptide-based solubilization surfactant part, DKDKC₁₂K, fand the other is the covalently connected linear polyacrylamide (PA) chain with different M_w values of 5, 7, or 18 kDa. Intermolecular interactions between the PA chains in DKDKC₁₂K-PA_n concentrated on the surfaces of membrane proteins via amphiphilic binding of the DKDKC₁₂K part to the integral membrane domain was observed. Therefore, DKDKC₁₂K-PA_n (n = 5, 7, and 18) could maintain a bound state even after removal of the unbound by ultrafiltration or gel-filtration chromatography. We used photosystem I (PSI) from Thermosynecoccus vulcanus as a representative to assess the impacts of new surfactants on the solubilized membrane protein structure and functions. Based on the maintenance of unique photophysical properties of PSI, we evaluated the ability of DKDKC₁₂K-PA_n (n = 5, 7, and 18) as a new solubilization surfactant.

SUBMITTER: Shimamoto T

PROVIDER: S-EPMC7913505 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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Design of PG-Surfactants Bearing Polyacrylamide Polymer Chain to Solubilize Membrane Proteins in a Surfactant-Free Buffer.

Shimamoto Taro T Nakakubo Tatsuki T Noji Tomoyasu T Koeda Shuhei S Kawakami Keisuke K Kamiya Nobuo N Mizuno Toshihisa T

International journal of molecular sciences 20210203 4

The development of techniques capable of using membrane proteins in a surfactant-free aqueous buffer is an attractive research area, and it should be elucidated for various membrane protein studies. To this end, we examined a method using new solubilization surfactants that do not detach from membrane protein surfaces once bound. The designed solubilization surfactants, DKDKC12K-PAn (n = 5, 7, and 18), consist of two parts: one is the lipopeptide-based solubil ...[more]

PMID: 33546366

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Project description:Due to the fact that surfactant molecules are known to alter the structure (and consequently the function) of a protein, protein-surfactant interactions are very important in the biological, pharmaceutical, and cosmetic industries. Although there are numerous studies on the interactions of albumins with surfactants, the investigations are often performed at fixed environmental conditions and limited to separate surface-active agents and consequently do not present an appropriate comparison between their different types and structures. In the present paper, the interactions between selected cationic, anionic, and nonionic surfactants, namely hexadecylpyridinium chloride (CPC), hexadecyltrimethylammonium bromide (CTAB), sodium dodecyl sulfate (SDS), polyethylene glycol sorbitan monolaurate, monopalmitate, and monooleate (TWEEN 20, TWEEN 40, and TWEEN 80, respectively) with bovine serum albumin (BSA) were studied qualitatively and quantitatively in an aqueous solution (10 mM cacodylate buffer; pH 5.0 and 7.0) by steady-state fluorescence spectroscopy supported by UV spectrophotometry and CD spectroscopy. Since in the case of all studied systems, the fluorescence intensity of BSA decreased regularly and significantly under the action of the surfactants added, the fluorescence quenching mechanism was analyzed thoroughly with the use of the Stern-Volmer equation (and its modification) and attributed to the formation of BSA-surfactant complexes. The binding efficiency and mode of interactions were evaluated among others by the determination, comparison, and discussion of the values of binding (association) constants of the newly formed complexes and the corresponding thermodynamic parameters (ΔG, ΔH, ΔS). Furthermore, the influence of the structure of the chosen surfactants (charge of hydrophilic head and length of hydrophobic chain) as well as different environmental conditions (pH, temperature) on the binding mode and the strength of the interaction has been investigated and elucidated.

Dataset Information

Design of PG-Surfactants Bearing Polyacrylamide Polymer Chain to Solubilize Membrane Proteins in a Surfactant-Free Buffer.

Publications

Design of PG-Surfactants Bearing Polyacrylamide Polymer Chain to Solubilize Membrane Proteins in a Surfactant-Free Buffer.

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