BibTex format
@article{Sadaf:2025:10.1021/acs.biomac.5c00036,
author = {Sadaf, A and Yun, HS and Lee, H and Stanfield, S and Lan, B and Salomon, K and Woubshete, M and Kim, S and Ehsan, M and Bae, H and Byrne, B and Loland, CJ and Liu, X and Guan, L and Im, W and Chae, PS},
doi = {10.1021/acs.biomac.5c00036},
journal = {Biomacromolecules},
title = {Multiple Pendants-Bearing Triglucosides for Membrane Protein Studies: Effects of Pendant Length and Number on Micelle Interior Hydration and Protein Stability.},
url = {http://dx.doi.org/10.1021/acs.biomac.5c00036},
year = {2025}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - Membrane proteins play central roles in cell physiology and are the targets of over 50% of FDA-approved drugs. In the present study, we prepared single alkyl-chained triglucosides decorated with multiple pendants, designated multiple pendant-bearing glucosides (MPGs), to enhance membrane protein stability. The new detergents feature two and four pendants of varying size at the hydrophilic-lipophilic interfaces, designated MPG-Ds and MPG-Ts, respectively. When tested with model membrane proteins, including the human adrenergic receptor (β2AR), the tetra-pendant-bearing MPGs (MPG-Ts) demonstrated superior performance compared to the dipendant analogs (MPG-Ds) and the gold standard DDM. All-atom molecular dynamics (MD) simulations results reveal that the four-pendant configuration of this detergent is remarkably effective in excluding water from the hydrophobic micelle interiors compared to the dipendant MPGs and DDM, an unprecedented feature of this new detergent. Our findings provide a novel strategy for designing water-resistant detergents, advancing the field of membrane protein research.
AU - Sadaf,A
AU - Yun,HS
AU - Lee,H
AU - Stanfield,S
AU - Lan,B
AU - Salomon,K
AU - Woubshete,M
AU - Kim,S
AU - Ehsan,M
AU - Bae,H
AU - Byrne,B
AU - Loland,CJ
AU - Liu,X
AU - Guan,L
AU - Im,W
AU - Chae,PS
DO - 10.1021/acs.biomac.5c00036
PY - 2025///
TI - Multiple Pendants-Bearing Triglucosides for Membrane Protein Studies: Effects of Pendant Length and Number on Micelle Interior Hydration and Protein Stability.
T2 - Biomacromolecules
UR - http://dx.doi.org/10.1021/acs.biomac.5c00036
UR - https://www.ncbi.nlm.nih.gov/pubmed/40087026
ER -