title: New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure-property relationships.
abstract: Detergents are widely used for membrane protein research; however, membrane proteins encapsulated in micelles formed by conventional detergents tend to undergo structural degradation, necessitating the development of new agents with enhanced efficacy. Here we prepared several hydrophobic variants of ganglio-tripod amphiphiles (TPAs) derived from previously reported TPAs and evaluated for a multi-subunit, pigment protein superassembly. In this study, TPA-16 was found to be most efficient in protein solubilization while TPA-15 proved most favourable in long-term protein stability. The current study combined with previous TPA studies enabled us to elaborate on a few detergent structure-property relationships that could provide useful guidelines for novel amphiphile design.
authors.affiliation: Department of Bionanotechnology, Hanyang University, Ansan, 426-791, Korea. pchae@hanyang.ac.kr.
authors.forename: Pil Seok
authors.initials: PS
authors.lastname: Chae
authors.forename: Hyoung Eun
authors.initials: HE
authors.lastname: Bae
authors.forename: Muhammad
authors.initials: M
authors.lastname: Ehsan
authors.forename: Hazrat
authors.initials: H
authors.lastname: Hussain
authors.forename: Jin Woong
authors.initials: JW
authors.lastname: Kim
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003902:Detergents / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008823:Micelles; D055550:Protein Stability; D016992:Rhodobacter / Q000737:chemistry*; D012995:Solubility; D013501:Surface-Active Agents / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D003902:Detergents; D008565:Membrane Proteins; D008823:Micelles; D013501:Surface-Active Agents