Size-dependent interaction of a 3-arm star poly(ethylene glycol) with two biological nanopores.
We use two pore-forming proteins, alpha-hemolysin and aerolysin, to compare the polymer size-dependence of ionic current block by two types of ethyleneglycol polymers: 1) linear and 2) 3-arm star poly(ethylene glycol), both applied as a polydisperse mixture of average mass 1kDa under high salt conditions. The results demonstrate that monomer size sensitivity, as known for linear PEGs, is conserved for the star polymers with only subtle differences in the dependence of the residual conductance on monomer number. To explain this absence of a dominant effect of polymer architecture, we propose that PEG adsorbs to the inner pore wall in a collapsed, salted-out state, likely due to the effect of hydrophobic residues in the pore wall on the availability of water for hydration.
['Talarimoghari|Monasadat|M|', 'Baaken|Gerhard|G|', 'Hanselmann|Ralf|R|', 'Behrends|Jan C|JC|']
D000327:Adsorption D001427:Bacterial Toxins D006460:Hemolysin Proteins D057927:Hydrophobic and Hydrophilic Interactions D058608:Nanopores D009994:Osmolar Concentration D011092:Polyethylene Glycols D052899:Pore Forming Cytotoxic Proteins D011485:Protein Binding
Polymers: From Adsorption to Translocation - Topical Issue in Memoriam Loïc Auvray (1956-2016)