ISSN:
1432-1017
Keywords:
Key words Ion channel
;
Transport
;
Polymers
;
Hydration
;
Water structure
;
Alpha hemolysin
;
Poly(ethylene glycol)
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract Electrostatic potentials created by fixed or induced charges regulate many cellular phenomena including the rate of ion transport through proteinaceous ion channels. Nanometer-scale pores of these channels also play a critical role in the transport of charged and neutral macromolecules. We demonstrate here that, surprisingly, changing the charge state of a channel markedly alters the ability of nonelectrolyte polymers to enter the channel's pore. Specifically, we show that the partitioning of differently-sized linear nonelectrolyte polymers of ethylene glycol into the Staphylococcus aureus α-hemolysin channel is altered by the solution pH. Protonating some of the channel side chains decreases the characteristic polymer size (molecular weight) that can enter the pore by ∼25% but increases the ionic current by ∼15%. Thus, the “steric” and “electric” size of the channel change in opposite directions. The results suggest that effects due to polymer and channel hydration are crucial for polymer transport through such pores.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002490050101
