Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study
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Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study. / Cho, Kyung Ho; Husri, Mohd; Amin, Anowarul; Gotfryd, Kamil; Lee, Ho Jin; Go, Juyeon; Kim, Jin Woong; Loland, Claus J; Guan, Lan; Byrne, Bernadette; Chae, Pil Seok.
In: The Analyst, Vol. 140, No. 9, 2015, p. 3157-63.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study
AU - Cho, Kyung Ho
AU - Husri, Mohd
AU - Amin, Anowarul
AU - Gotfryd, Kamil
AU - Lee, Ho Jin
AU - Go, Juyeon
AU - Kim, Jin Woong
AU - Loland, Claus J
AU - Guan, Lan
AU - Byrne, Bernadette
AU - Chae, Pil Seok
PY - 2015
Y1 - 2015
N2 - 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-β-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.
AB - 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-β-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.
U2 - 10.1039/c5an00240k
DO - 10.1039/c5an00240k
M3 - Journal article
C2 - 25813698
VL - 140
SP - 3157
EP - 3163
JO - The Analyst
JF - The Analyst
SN - 0003-2654
IS - 9
ER -
ID: 137623574