A comparison of SMA (styrene maleic acid) and DIBMA (di-isobutylene maleic acid) for membrane protein purification | Health & Environmental Research Online (HERO)

HERO ID

6592389

Reference Type

Journal Article

Title

A comparison of SMA (styrene maleic acid) and DIBMA (di-isobutylene maleic acid) for membrane protein purification

Author(s)

Gulamhussein, AA; Uddin, R; Tighe, BJ; Poyner, DR; Rothnie, AJ; ,

Year

2020

Is Peer Reviewed?

1

Journal

Biochimica et Biophysica Acta. Biomembranes
ISSN: 0005-2736
EISSN: 1879-2642

Publisher

ELSEVIER

Location

AMSTERDAM

Volume

1862

Issue

7

Page Numbers

183281-

Language

English

PMID

32209303

DOI

10.1016/j.bbamem.2020.183281

Web of Science Id

WOS:000528196600010

URL

https://www.scopus.com/inward/record.uri?eid=2-s2.0-85082775364&doi=10.1016%2fj.bbamem.2020.183281&partnerID=40&md5=9d8048efd4c04256809f6836b73cb409
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Abstract

The use of styrene maleic acid co-polymer (SMA) for membrane protein extraction and purification has grown in recent years. SMA inserts in the membrane and assembles into small discs of bilayer encircled by polymer, termed SMA lipid particles (SMALPs). This allows purification of membrane proteins whilst maintaining their lipid bilayer environment. SMALPs offer several improvements over conventional detergent approaches, however there are limitations, most notably a sensitivity to low pH and divalent cations. Recently it was shown that the aliphatic diisobutylene-maleic acid (DIBMA) copolymer, was also able to directly solubilise membranes forming DIBMALPs (DIBMA lipid particles), and that this polymer overcame some of the limitations of SMA. In this study the ability of DIBMA to solubilise and purify functional membrane proteins has been compared to SMA. It was found that DIBMA is able to solubilise several different membrane proteins from different expression systems, however for some proteins it gives a lower yield and lower degree of purity than SMA. DIBMA extracted G protein-coupled receptors retain ligand- and G protein-binding. DIBMALPS are larger than SMALPs and display a decreased sensitivity to magnesium. However the stability of DIBMALPs appears to be lower than SMALPs. The lower purity and lower stability are likely linked to the larger size of the DIBMALP particle. However, this also offers a potentially less rigid lipid environment which may be more amenable to protein dynamics. Therefore the optimal choice of polymer will depend on which features of a protein are to be investigated.

Keywords

ABC transporter; DIBMALP; GPCR; Membrane protein; SMALP

Series

Biochimica et biophysica acta. Biomembranes