Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 채필석 | - |
dc.date.accessioned | 2022-08-29T05:51:27Z | - |
dc.date.available | 2022-08-29T05:51:27Z | - |
dc.date.issued | 2021-07 | - |
dc.identifier.citation | ACTA BIOMATERIALIA, v. 128, Page. 393-407 | en_US |
dc.identifier.issn | 1742-7061 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S1742706121002877 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/172588 | - |
dc.description.abstract | Membrane protein structures provide atomic level insight into essential biochemical processes and facilitate protein structure-based drug design. However, the inherent instability of these bio-macromolecules outside lipid bilayers hampers their structural and functional study. Detergent micelles can be used to solubilize and stabilize these membrane-inserted proteins in aqueous solution, thereby enabling their downstream characterizations. Membrane proteins encapsulated in detergent micelles tend to denature and aggregate over time, highlighting the need for development of new amphiphiles effective for protein solubility and stability. In this work, we present newly-designed maltoside detergents containing a pendant chain attached to a glycerol-decorated tris(hydroxymethyl)methane (THM) core, designated GTMs. One set of the GTMs has a hydrophobic pendant (ethyl chain; E-GTMs), and the other set has a hydrophilic pendant (methoxyethoxylmethyl chain; M-GTMs) placed in the hydrophobic-hydrophilic interfaces. The two sets of GTMs displayed profoundly different behaviors in terms of detergent self-assembly and protein stabilization efficacy. These behaviors mainly arise from the polarity difference between two pendants (ethyl and methoxyethoxylmethyl chains) that results in a large variation in detergent conformation between these sets of GTMs in aqueous media. The resulting high hydrophobic density in the detergent micelle interior is likely responsible for enhanced efficacy of the M-GTMs for protein stabilization compared to the E-GTMs and a gold standard detergent DDM. A representative GTM, M-GTM-O12, was more effective for protein stability than some recently developed detergents including LMNG. This is the first case study investigating the effect of pendant polarity on detergent geometry correlated with detergent efficacy for protein stabilization. | en_US |
dc.description.sponsorship | This work was supported by LG Yonam Foundation of Ko- rea (P.S.C.). This work was also supported by the National Research Foundation of Korea (NRF) (2021R1A2C2006067 and 2018R1A6A1A03024231 to P.S.C.). This study was also supported by the National Science Foundation (grant MCB-1810695 to W.I.) and the National Institutes of Health (grants R01GM122759 and R21NS105863 to L.G.). S.K. and Y.U. were supported by an individ- ual grant of Korea Institute for Advanced Study (CG080501) and the Research Clerkship Program of Nara Medical University, Japan, respectively. | en_US |
dc.language.iso | en | en_US |
dc.publisher | ELSEVIER SCI LTD | en_US |
dc.subject | Pendant polarity | en_US |
dc.subject | Detergent conformation | en_US |
dc.subject | Membrane proteins | en_US |
dc.subject | Protein stabilization | en_US |
dc.subject | Amphiphile design | en_US |
dc.title | Conformationally flexible core-bearing detergents with a hydrophobic or hydrophilic pendant: Effect of pendant polarity on detergent conformation and membrane protein stability | en_US |
dc.type | Article | en_US |
dc.relation.volume | 128 | - |
dc.identifier.doi | 10.1016/j.actbio.2021.04.043 | - |
dc.relation.page | 393-407 | - |
dc.relation.journal | ACTA BIOMATERIALIA | - |
dc.contributor.googleauthor | Sadaf, Aiman | - |
dc.contributor.googleauthor | Kim, Seonghoon | - |
dc.contributor.googleauthor | Bae, Hyoung Eun | - |
dc.contributor.googleauthor | Wang, Haoqing | - |
dc.contributor.googleauthor | Nygaard, Andreas | - |
dc.contributor.googleauthor | Uegaki, Yuki | - |
dc.contributor.googleauthor | Du, Yang | - |
dc.contributor.googleauthor | Munk, Chastine F. | - |
dc.contributor.googleauthor | Katsube, Satoshi | - |
dc.contributor.googleauthor | Sung Lee, Hyun | - |
dc.contributor.googleauthor | Bae, Jungnam | - |
dc.contributor.googleauthor | Choi, Chul Won | - |
dc.contributor.googleauthor | Choi, Hee-Jung | - |
dc.contributor.googleauthor | Byrne, Bernadette | - |
dc.contributor.googleauthor | Gellman, Samuel H. | - |
dc.contributor.googleauthor | Guan, Lan | - |
dc.contributor.googleauthor | Loland, Claus J. | - |
dc.contributor.googleauthor | Kobilka, Brian K. | - |
dc.contributor.googleauthor | Im, Wonpil | - |
dc.contributor.googleauthor | Chae, Pil Seok | - |
dc.relation.code | 2021005664 | - |
dc.sector.campus | E | - |
dc.sector.daehak | COLLEGE OF ENGINEERING SCIENCES[E] | - |
dc.sector.department | DEPARTMENT OF BIONANO ENGINEERING | - |
dc.identifier.pid | pchae | - |
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