期刊
ANALYST
卷 140, 期 9, 页码 3157-3163出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5an00240k
关键词
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资金
- National Research Foundation of Korea (NRF) - Korean government (MSIP) [2008-0061891, 2013R1A2A2A03067623]
- Biotechnology and Biological Sciences Research Council [BB/K017292/1]
- National Science Foundation [MCB-1158085]
- Norman Hackerman Advanced Research Program [010674-0034-2009]
- National Institutes of Health [R01 GM095538]
- Danish Council for Independent Research - Sapere Aude
- Lundbeck Foundation
- UNIK Center for Synthetic Biology
- National Research Foundation of Korea [2013R1A2A2A03067623] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Biotechnology and Biological Sciences Research Council [BB/K017292/1] Funding Source: researchfish
- BBSRC [BB/K017292/1] Funding Source: UKRI
Detergents are typically used to both extract membrane proteins (MPs) from the lipid bilayers and maintain them in solution. However, MPs encapsulated in detergent micelles are often prone to denaturation and aggregation. Thus, the development of novel agents with enhanced stabilization characteristics is necessary to advance MP research. Maltose neopentyl glycol-3 (MNG-3) has contributed to >10 crystal structures including G-protein coupled receptors. Here, we prepared MNG-3 analogues and characterised their properties using selected MPs. Most MNGs were superior to a conventional detergent, n-dodecyl-beta-D-maltopyranoside (DDM), in terms of membrane protein stabilization efficacy. Interestingly, optimal stabilization was achieved with different MNG-3 analogues depending on the target MP. The origin for such detergent specificity could be explained by a novel concept: compatibility between detergent hydrophobicity and MP tendency to denature and aggregate. This set of MNGs represents viable alternatives to currently available detergents for handling MPs, and can be also used as tools to estimate MP sensitivity to denaturation and aggregation.
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