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- 저자 : Molist, Iago (검색결과 2 건)
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Vitamin E-based glycoside amphiphiles for membrane protein structural studies
Ehsan, Muhammad,Du, Yang,Molist, Iago,Seven, Alpay B.,Hariharan, Parameswaran,Mortensen, Jonas S.,Ghani, Lubna,Loland, Claus J.,Skiniotis, Georgios,Guan, Lan,Byrne, Bernadette,Kobilka, Brian K.,Chae, The Royal Society of Chemistry 2018 Organic & Biomolecular Chemistry Vol.16 No.14
<P>Membrane proteins play critical roles in a variety of cellular processes. For a detailed molecular level understanding of their biological functions and roles in disease, it is necessary to extract them from the native membranes. While the amphipathic nature of these bio-macromolecules presents technical challenges, amphiphilic assistants such as detergents serve as useful tools for membrane protein structural and functional studies. Conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus it is essential to develop novel agents with enhanced properties. Here, we designed and characterized a novel class of amphiphiles with vitamin E (<I>i.e.</I>, α-tocopherol) as the hydrophobic tail group and saccharide units as the hydrophilic head group. Designated vitamin E-based glycosides (VEGs), these agents were evaluated for their ability to solubilize and stabilize a set of membrane proteins. VEG representatives not only conferred markedly enhanced stability to a diverse range of membrane proteins compared to conventional detergents, but VEG-3 also showed notable efficacy toward stabilization and visualization of a membrane protein complex. In addition to hydrophile-lipophile balance (HLB) of detergent molecules, the chain length and molecular geometry of the detergent hydrophobic group seem key factors in determining detergent efficacy for membrane protein (complex) stability.</P>
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Dendronic trimaltoside amphiphiles (DTMs) for membrane protein study
Sadaf, Aiman,Du, Yang,Santillan, Claudia,Mortensen, Jonas S.,Molist, Iago,Seven, Alpay B.,Hariharan, Parameswaran,Skiniotis, Georgios,Loland, Claus J.,Kobilka, Brian K.,Guan, Lan,Byrne, Bernadette,Cha Royal Society of Chemistry 2017 Chemical Science Vol.8 No.12
<▼1><P>A novel amphiphile with a dendronic hydrophobic group (DTM-A6) was markedly effective at stabilizing and visualizing a GPCR-G<SUB>s</SUB> complex.</P></▼1><▼2><P>The critical contribution of membrane proteins in normal cellular function makes their detailed structure and functional analysis essential. Detergents, amphipathic agents with the ability to maintain membrane proteins in a soluble state in aqueous solution, have key roles in membrane protein manipulation. Structural and functional stability is a prerequisite for biophysical characterization. However, many conventional detergents are limited in their ability to stabilize membrane proteins, making development of novel detergents for membrane protein manipulation an important research area. The architecture of a detergent hydrophobic group, that directly interacts with the hydrophobic segment of membrane proteins, is a key factor in dictating their efficacy for both membrane protein solubilization and stabilization. In the current study, we developed two sets of maltoside-based detergents with four alkyl chains by introducing dendronic hydrophobic groups connected to a trimaltoside head group, designated dendronic trimaltosides (DTMs). Representative DTMs conferred enhanced stabilization to multiple membrane proteins compared to the benchmark conventional detergent, DDM. One DTM (<I>i.e.</I>, DTM-A6) clearly outperformed DDM in stabilizing human β<SUB>2</SUB> adrenergic receptor (β<SUB>2</SUB>AR) and its complex with G<SUB>s</SUB> protein. A further evaluation of this DTM led to a clear visualization of β<SUB>2</SUB>AR-G<SUB>s</SUB> complex <I>via</I> electron microscopic analysis. Thus, the current study not only provides novel detergent tools useful for membrane protein study, but also suggests that the dendronic architecture has a role in governing detergent efficacy for membrane protein stabilization.</P></▼2>
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