A monodisperse transmembrane α-helical peptide barrel (original) (raw)

• Woolfson, D. N. The design of coiled-coil structures and assemblies. Adv. Protein Chem. 70, 79–112 (2005).
  CAS PubMed Google Scholar
• Woolfson, D. N. et al. De novo protein design: how do we expand into the universe of possible protein structures? Curr. Opin. Struct. Biol. 33, 16–26 (2015).
  CAS PubMed Google Scholar
• Woolfson, D. N., Bartlett, G. J., Bruning, M. & Thomson, A. R. New currency for old rope: from coiled-coil assemblies to alpha-helical barrels. Curr. Opin. Struct. Biol. 22, 432–441 (2012).
  CAS PubMed Google Scholar
• Lear, J. D., Wasserman, Z. R. & DeGrado, W. F. Synthetic amphiphilic peptide models for protein ion channels. Science 240, 1177–1181 (1988).
  CAS PubMed Google Scholar
• Joh, N. H. et al. De novo design of a transmembrane Zn2+-transporting four-helix bundle. Science 346, 1520–1524 (2014).
  CAS PubMed PubMed Central Google Scholar
• Franceschini, L., Soskine, M., Biesemans, A. & Maglia, G. A nanopore machine promotes the vectorial transport of DNA across membranes. Nat. Commun. 4, 2415 (2013).
  PubMed PubMed Central Google Scholar
• Bayley, H. Membrane-protein structure: piercing insights. Nature 459, 651–652 (2009).
  CAS PubMed Google Scholar
• Dong, C. et al. Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein. Nature 444, 226–229 (2006).
  Article CAS Google Scholar
• Kong, L. et al. Single-molecule interrogation of a bacterial sugar transporter allows the discovery of an extracellular inhibitor. Nat. Chem. 5, 651–659 (2013).
  CAS PubMed Google Scholar
• Soskine, M. et al. An engineered ClyA nanopore detects folded target proteins by selective external association and pore entry. Nano Lett. 12, 4895–4900 (2012).
  CAS PubMed PubMed Central Google Scholar
• Soskine, M., Biesemans, A., De Maeyer, M. & Maglia, G. Tuning the size and properties of ClyA nanopores assisted by directed evolution. J. Am. Chem. Soc. 135, 13456–13463 (2013).
  CAS PubMed PubMed Central Google Scholar
• Tanaka, K., Caaveiro, J. M., Morante, K., González-Mañas, J. M. & Tsumoto, K. Structural basis for self-assembly of a cytolytic pore lined by protein and lipid. Nat. Commun. 6, 6337 (2015).
  PubMed PubMed Central Google Scholar
• Zaccai, N. R. et al. A de novo peptide hexamer with a mutable channel. Nat. Chem. Biol. 7, 935–941 (2011).
  CAS PubMed PubMed Central Google Scholar
• Thomson, A. R. et al. Computational design of water-soluble alpha-helical barrels. Science 346, 485–488 (2014).
  CAS PubMed Google Scholar
• Bayley, H. Designed membrane channels and pores. Curr. Opin. Biotechnol. 10, 94–103 (1999).
  CAS PubMed Google Scholar
• Bayley, H. & Jayasinghe, L. Functional engineered channels and pores (Review). Mol. Membr. Biol. 21, 209–220 (2004).
  CAS PubMed Google Scholar
• Majd, S. et al. Applications of biological pores in nanomedicine, sensing, and nanoelectronics. Curr. Opin. Biotechnol. 21, 439–476 (2010).
  CAS PubMed PubMed Central Google Scholar
• Braha, O. et al. Designed protein pores as components for biosensors. Chem. Biol. 4, 497–505 (1997).
  CAS PubMed Google Scholar
• Bayley, H. & Cremer, P. S. Stochastic sensors inspired by biology. Nature 413, 226–230 (2001).
  CAS PubMed Google Scholar
• Bayley, H. Nanopore sequencing: from imagination to reality. Clin. Chem. 61, 25–31 (2015).
  CAS PubMed Google Scholar
• Jain, M. et al. Improved data analysis for the MinION nanopore sequencer. Nat. Methods 12, 351–356 (2015).
  CAS PubMed PubMed Central Google Scholar
• Song, L. et al. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274, 1859–1866 (1996).
  CAS PubMed Google Scholar
• Gu, L. Q., Braha, O., Conlan, S., Cheley, S. & Bayley, H. Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter. Nature 398, 686–690 (1999).
  CAS PubMed Google Scholar
• Banerjee, A. et al. Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores. Proc. Natl Acad. Sci. USA 107, 8165–8170 (2010).
  CAS Google Scholar
• Walshaw, J. & Woolfson, D. N. Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 307, 1427–1450 (2001).
  CAS PubMed Google Scholar
• van den Berg, B., Prathyusha Bhamidimarri, S., Dahyabhai Prajapati, J., Kleinekathöfer, U. & Winterhalter, M. Outer-membrane translocation of bulky small molecules by passive diffusion. Proc. Natl Acad. Sci. USA 112, E2991–E2999 (2015).
  CAS PubMed Google Scholar
• Doyle, D. A. et al. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science 280, 69–77 (1998).
  CAS PubMed Google Scholar
• Mueller, M., Grauschopf, U., Maier, T., Glockshuber, R. & Ban, N. The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature 459, 726–730 (2009).
  CAS PubMed Google Scholar
• Miles, G., Movileanu, L. & Bayley, H. Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore. Protein Sci. 11, 894–902 (2002).
  CAS PubMed PubMed Central Google Scholar
• Smart, O. S., Breed, J., Smith, G. R. & Sansom, M. S. A novel method for structure-based prediction of ion channel conductance properties. Biophys. J. 72, 1109–1126 (1997).
  CAS PubMed PubMed Central Google Scholar
• Sukharev, S., Betanzos, M., Chiang, C. S. & Guy, H. R. The gating mechanism of the large mechanosensitive channel MscL. Nature 409, 720–724 (2001).
  CAS PubMed Google Scholar
• Wang, Y. et al. Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel. eLife 3, e01834 (2014).
  PubMed PubMed Central Google Scholar
• Pliotas, C . et al. The role of lipids in mechanosensation. Nat. Struct. Mol. Biol. 22, 991–8 (2015).
  CAS PubMed PubMed Central Google Scholar
• Walker, B., Krishnasastry, M., Zorn, L. & Bayley, H. Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis. J. Biol. Chem. 267, 21782–6 (1992).
  CAS PubMed Google Scholar
• Walker, B., Braha, O., Cheley, S. & Bayley, H. An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem. Biol. 2, 99–105 (1995).
  CAS PubMed Google Scholar
• Dunstone, M. A. & Tweten, R. K. Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr. Opin. Struct. Biol. 22, 342–349 (2012).
  CAS PubMed PubMed Central Google Scholar
• Leung, C. et al. Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin. eLife 3, e04247 (2014).
  PubMed PubMed Central Google Scholar
• Stoddart, D. et al. Functional truncated membrane pores. Proc. Natl Acad. Sci. USA 111, 2425–2430 (2014).
  CAS PubMed Google Scholar
• Karginov, V. A. Cyclodextrin derivatives as anti-infectives. Curr. Opin. Pharmacol. 13, 717–725 (2013).
  CAS PubMed Google Scholar
• Brogden, K. A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238–250 (2005).
  CAS PubMed Google Scholar
• Cirac, A. D. et al. The molecular basis for antimicrobial activity of pore-forming cyclic peptides. Biophys. J. 100, 2422–2431 (2011).
  CAS PubMed PubMed Central Google Scholar
• Song, C. et al. Crystal structure and functional mechanism of a human antimicrobial membrane channel. Proc. Natl Acad. Sci. USA 110, 4586–4591 (2013).
  CAS PubMed Google Scholar
• Haswell, E. S., Phillips, R. & Rees, D. C. Mechanosensitive channels: what can they do and how do they do it? Structure 19, 1356–1369 (2011).
  CAS PubMed PubMed Central Google Scholar
• Naismith, J. H. & Booth, I. R. Bacterial mechanosensitive channels—MscS: evolution's solution to creating sensitivity in function. Annu. Rev. Biophys. 41, 157–177 (2012).
  CAS PubMed PubMed Central Google Scholar
• Lee, J. & Bayley, H. Semisynthetic protein nanoreactor for single-molecule chemistry. Proc. Natl Acad. Sci. USA 112, 13768–13773 (2015).
  CAS PubMed Google Scholar
• Fernandez-Lopez, S. et al. Antibacterial agents based on the cyclic D,L-alpha-peptide architecture. Nature 412, 452–455 (2001).
  CAS PubMed Google Scholar
• Fjell, C. D., Hiss, J. A., Hancock, R. E. & Schneider, G. Designing antimicrobial peptides: form follows function. Nat. Rev. Drug. Discov. 11, 37–51 (2012).
  CAS Google Scholar
• Hoskin, D. W. & Ramamoorthy, A. Studies on anticancer activities of antimicrobial peptides. Biochim. Biophys. Acta 1778, 357–375 (2008).
  CAS PubMed Google Scholar
• Gaspar, D., Veiga, A. S. & Castanho, M. A. From antimicrobial to anticancer peptides. A review. Front. Microbiol. 4, 294 (2013).
  PubMed PubMed Central Google Scholar
• Mantri, S., Tanuj Sapra, K., Cheley, S., Sharp, T. H. & Bayley, H. An engineered dimeric protein pore that spans adjacent lipid bilayers. Nat. Commun. 4, 1725 (2013).
  PubMed PubMed Central Google Scholar
• Gutsmann, T., Heimburg, T., Keyser, U., Mahendran, K. R. & Winterhalter, M. Protein reconstitution into freestanding planar lipid membranes for electrophysiological characterization. Nat. Protoc. 10, 188–198 (2015).
  PubMed Google Scholar