Bacterial Channels

Membrane permeability barriers are among the factors contributing to the intrinsic resistance of bacteria to antibiotics. For example, it is well established that the general porin of the outer bacterial membrane, OmpF, is the pathway for penicillins to the periplasmic space. Therefore, understanding transport through bacterial channels is important for the design of new, efficient anti-bacterial drugs.

Related references:

A. Alcaraz, E.M. Nestorovich, M. Aguilella-Arzo, V.M. Aguilella , and S.M. Bezrukov. Salting out the ionic selectivity of a wide channel: The asymmetry of OmpF. Biophysical Journal, 2004, 87:943-957. [PDF]

E.M. Nestorovich, T.K. Rostovtseva, and S.M. Bezrukov. Residue ionization and ion transport through OmpF channels. Biophysical Journal, 2003, 85 :3718-3729. [PDF]

E.M. Nestorovich, C. Danelon, M. Winterhalter, and S.M. Bezrukov. Designed to penetrate: Time-resolved interaction of single antibiotic molecules with bacterial pores. Proc. Natl. Acad. Sci. USA , 2002, 99:9789-9794. [PDF]

T.K. Rostovtseva, E.M. Nestorovich, and S.M. Bezrukov. Partitioning of differently sized poly(ethylene glycol)s into OmpF porin. Biophysical Journal, 2002, 82:160-169. [PDF]

L. Kullman, M. Winterhalter, and S.M. Bezrukov. Transport of maltodextrins through maltoporin: A single-channel study. Biophysical Journal, 2002, 82: 803-812. [PDF]

M. Winterhalter, C. Hilty, S.M. Bezrukov, C. Nardin, W. Meier , and D. Fournier. Controlling membrane permeability with bacterial porins: Application to encapsulated enzymes. Talanta, 2001, 55:965-971. [PDF]

S.M. Bezrukov, L. Kullman, and M. Winterhalter. Probing sugar translocation through maltoporin at the single channel level. FEBS Letters , 2000, 476:224-228. [PDF]