The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria
- J. Pagés, Chloe E. James, M. Winterhalter
- BiologyNature Reviews Microbiology
- 1 December 2008
The bacterial response towards antibiotic stress on altered membrane permeability is outlined and recent advances in molecular approaches that are improving knowledge of the physico-chemical parameters that govern the translocation of antibiotics through porin channels are discussed.
Designed to penetrate: Time-resolved interaction of single antibiotic molecules with bacterial pores
- E. M. Nestorovich, C. Danelon, M. Winterhalter, S. Bezrukov
- BiologyProceedings of the National Academy of Sciences…
- 15 July 2002
It is hypothesized that, in analogy to substrate-specific channels that evolved to bind certain metabolite molecules, antibiotics have “evolved” to be channel-specific.
Structural basis for nutrient acquisition by dominant members of the human gut microbiota
- A. J. Glenwright, K. Pothula, B. Berg
- BiologyNature
- 19 January 2017
X-ray crystal structures of two functionally distinct SusCD complexes purified from Bacteroides thetaiotaomicron are presented and a general model for substrate translocation is derived to provide mechanistic insights into outer membrane nutrient import by members of the microbiota, an area of major importance for understanding human–microbiota symbiosis.
Protein encapsulation in liposomes: efficiency depends on interactions between protein and phospholipid bilayer.
- J. Colletier, B. Chaize, M. Winterhalter, D. Fournier
- BiologyBMC Biotechnology
- 10 May 2002
By increasing the lipid concentration, increasing the number of freeze-thaw cycles and enhancing the interactions of the enzyme with the liposome lipid surface more than 40% of the initial total activity can be encapsulated.
How β-Lactam Antibiotics Enter Bacteria: A Dialogue with the Porins
- Chloe E. James, Kozhinjampara R. Mahendran, J. Pagés
- BiologyPLoS ONE
- 12 May 2009
The idea of a molecular “passport” that allows rapid transport of substrates through porins is proposed that may hold the key for the next generation of antibiotics capable of rapid intracellular accumulation to circumvent the further development MDR infections.
Amphiphilic block copolymer nanocontainers as bioreactors
- C. Nardin, J. Widmer, M. Winterhalter, W. Meier
- Biology
- 1 April 2001
Surprisingly, the proteins remain functional despite the extreme thickness of the membranes and that even after polymerization of the reactive triblock copolymers, which opens a new field to create mechanically stable protein/polymer hybrid membranes.
Transport of maltodextrins through maltoporin: a single-channel study.
- L. Kullman, M. Winterhalter, S. Bezrukov
- BiologyBiophysical Journal
- 1 February 2002
Kinetics of pore size during irreversible electrical breakdown of lipid bilayer membranes.
- C. Wilhelm, M. Winterhalter, U. Zimmermann, R. Benz
- Physics, BiologyBiophysical Journal
- 1993
The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity.
- R. Brok, P. van Gelder, W. Bitter
- Biology, ChemistryJournal of Molecular Biology
- 17 December 1999
Results demonstrate that the C-terminal secretin homology domain of XcpQ is the structural domain that forms the channel through which macromolecules are being transported.
Nanoreactors based on (polymerized) ABA-triblock copolymer vesicles
- C. Nardin, S. Thoeni, J. Widmer, M. Winterhalter, W. Meier
- Materials Science
- 2000
A new kind of nanoreactor has been prepared by the
incorporation of a channel protein into the shell of (polymerized) vesicles
formed from an amphiphilic ABA-triblock copolymer.
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