Examining the stability of membrane proteins within SMALPs

Autor: Aiman A. Gulamhussein, Timothy R. Dafforn, Zakaria Saidani, Simran Lallie, Lai Ki Chiu, Monique K. Liddar, Alice Rothnie, Stephen Hall, Stephen Fenner, Danyall Meah, Sabiha S. Sumar, Aneel Akram, Damian D. Soja, Ashlyn Mathews, Jaimin H. Patel, Hannah Healy, Culum Painter, Zain Mohammed, Nabeel Hussain
Rok vydání: 2019
Předmět:
Zdroj: European Polymer Journal. 112:120-125
ISSN: 0014-3057
1873-1945
DOI: 10.1016/j.eurpolymj.2018.12.008
Popis: Amphipathic co-polymers such as styrene-maleic acid (SMA) have gained popularity over the last few years due to their ability and ease of use in solubilising and purifying membrane proteins in comparison to conventional methods of extraction such as detergents. SMA2000 is widely used for membrane protein studies and is considered as the optimal polymer for this technique. In this study a side-by-side comparison of SMA2000 with the polymer SZ30010 was carried out as both these polymers have similar styrene:maleic acid ratios and average molecular weights. Ability to solubilise, purify and stabilise membrane proteins was tested using three structurally different membrane proteins. Our results show that both polymers can be used to extract membrane proteins at a comparable efficiency to conventional detergent dodecylmaltoside (DDM). SZ30010 was found to give a similar protein yield and, SMALP disc size as SMA2000, and both polymers offered an increased purity and increased thermostability compared to DDM. Further investigation was conducted to investigate SMALP sensitivity to divalent cations. It was found that the sensitivity is polymer specific and not dependent on the protein encapsulated. Neither is it affected by the concentration of SMALPs. Larger divalent cations such as Co2+ and Zn2+ resulted in an increased sensitivity.
Databáze: OpenAIRE
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