Hagan Bayley

Last updated

Hagan Bayley
Born
John Hagan Pryce Bayley

(1951-02-13) 13 February 1951 (age 73) [1]
Wales, UK
Alma mater
Known for
Awards FRS (2011) [3]
Scientific career
Fields Chemical Biology
Institutions
Thesis Adamantylidene: A Hydrophobic, Photogenerated Reagent for the Characterization of Intrinsic Membrane Proteins  (1979)
Doctoral advisor Jeremy Knowles [4]
Website bayley.chem.ox.ac.uk

John Hagan Pryce Bayley FRS, FLSW (born 13 February 1951 [1] ) is a British scientist, who holds the position of Professor of Chemical Biology at the University of Oxford. [5] [6] [7] [8] [9]

Contents

Life and education

Bayley was educated at The King's School, Chester and [1] Uppingham School, before going to Balliol College, Oxford in 1970 [10] and Harvard University, where he was awarded a Ph.D. in 1979. [4] [11]

Originally from Wales, he spent much of his early career between the United Kingdom and the United States. [12]

Research

Bayley's research is largely based on the study and engineering of transmembrane pore-forming proteins, [13] as well as interests in chemical signal transduction and biomolecular materials. [14] He is the co-founder of Oxford Nanopore Technologies Ltd. Bayley's research includes work on the pore-forming protein alpha haemolysin [15] engineered for sensing has been highly cited. [16]

Career

Following his PhD, Bayley completed postdoctoral research at Massachusetts Institute of Technology. [4] He previously held appointments at Columbia University, University of Massachusetts Medical School, and Texas A&M University. [4] Bayley has been based at the University of Oxford since 2003 and is a fellow of Hertford College, Oxford. [17]

Awards and honours

Bayley was elected a Fellow of the Royal Society in 2011. [3] His nomination reads

Hagan Bayley's achievements lie at the interface between chemistry and biology. He has used protein chemistry, organic chemistry, and biophysics to explore the folding, assembly, and function of transmembrane channels and pores. These studies have led to the development of protein pores as "nanoreactors", with which both non-covalent and covalent chemistry of single molecules can be examined. Applications of this methodology have included host–guest interactions and step-by-step polymer growth. Based on this work, Bayley has developed "stochastic sensing," which has been shown with a wide variety of analytes to reveal both concentration and identity through single-molecule detection. [3]

In 2012, Bayley was elected as a Fellow of the Learned Society of Wales. [18]

The Science Council recognised him as "one of the UK's 100 leading practising scientists" of 2014. [19]

Related Research Articles

<span class="mw-page-title-main">Post-translational modification</span> Chemical changes in proteins following their translation from mRNA

In molecular biology, post-translational modification (PTM) is the covalent process of changing proteins following protein biosynthesis. PTMs may involve enzymes or occur spontaneously. Proteins are created by ribosomes, which translate mRNA into polypeptide chains, which may then change to form the mature protein product. PTMs are important components in cell signalling, as for example when prohormones are converted to hormones.

<span class="mw-page-title-main">Nanopore</span>

A nanopore is a pore of nanometer size. It may, for example, be created by a pore-forming protein or as a hole in synthetic materials such as silicon or graphene.

<span class="mw-page-title-main">Nanopore sequencing</span> DNA / RNA sequencing technique

Nanopore sequencing is a third generation approach used in the sequencing of biopolymers — specifically, polynucleotides in the form of DNA or RNA.

<span class="mw-page-title-main">Potassium channel</span> Ion channel that selectively passes K+

Potassium channels are the most widely distributed type of ion channel found in virtually all organisms. They form potassium-selective pores that span cell membranes. Potassium channels are found in most cell types and control a wide variety of cell functions.

<span class="mw-page-title-main">P2X purinoreceptor</span> Group of ion channel proteins

The P2X receptors, also ATP-gated P2X receptor cation channel family, is a protein family that consists of cation-permeable ligand-gated ion channels that open in response to the binding of extracellular adenosine 5'-triphosphate (ATP). They belong to a larger family of receptors known as the ENaC/P2X superfamily. ENaC and P2X receptors have similar 3-D structures and are homologous. P2X receptors are present in a diverse array of organisms including humans, mouse, rat, rabbit, chicken, zebrafish, bullfrog, fluke, and amoeba.

<span class="mw-page-title-main">Dystroglycan</span> Protein

Dystroglycan is a protein that in humans is encoded by the DAG1 gene.

<span class="mw-page-title-main">Mitochondrial membrane transport protein</span>

Mitochondrial membrane transport proteins, also known as mitochondrial carrier proteins, are proteins which exist in the membranes of mitochondria. They serve to transport molecules and other factors, such as ions, into or out of the organelles. Mitochondria contain both an inner and outer membrane, separated by the inter-membrane space, or inner boundary membrane. The outer membrane is porous, whereas the inner membrane restricts the movement of all molecules. The two membranes also vary in membrane potential and pH. These factors play a role in the function of mitochondrial membrane transport proteins. There are 53 discovered human mitochondrial membrane transporters, with many others that are known to still need discovered.

<span class="mw-page-title-main">Pore-forming toxin</span> Protein-produced toxins that create pores in cell membrane

Pore-forming proteins are usually produced by bacteria, and include a number of protein exotoxins but may also be produced by other organisms such as apple snails that produce perivitellin-2 or earthworms, who produce lysenin. They are frequently cytotoxic, as they create unregulated pores in the membrane of targeted cells.

Cell-penetrating peptides (CPPs) are short peptides that facilitate cellular intake and uptake of molecules ranging from nanosize particles to small chemical compounds to large fragments of DNA. The "cargo" is associated with the peptides either through chemical linkage via covalent bonds or through non-covalent interactions.

<span class="mw-page-title-main">Hemolysin</span> Molecule destroying the membrane of red blood cells

Hemolysins or haemolysins are lipids and proteins that cause lysis of red blood cells by disrupting the cell membrane. Although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infection. However, hemolysins are often capable of lysing red blood cells in vitro.

<span class="mw-page-title-main">Nanofluidics</span> Dynamics of fluids confined in nanoscale structures

Nanofluidics is the study of the behavior, manipulation, and control of fluids that are confined to structures of nanometer characteristic dimensions. Fluids confined in these structures exhibit physical behaviors not observed in larger structures, such as those of micrometer dimensions and above, because the characteristic physical scaling lengths of the fluid, very closely coincide with the dimensions of the nanostructure itself.

<span class="mw-page-title-main">Thiamine transporter 1</span> Mammalian protein found in Homo sapiens

Thiamine transporter 1, also known as thiamine carrier 1 (TC1) or solute carrier family 19 member 2 (SLC19A2) is a protein that in humans is encoded by the SLC19A2 gene. SLC19A2 is a thiamine transporter. Mutations in this gene cause thiamine-responsive megaloblastic anemia syndrome (TRMA), which is an autosomal recessive disorder characterized by diabetes mellitus, megaloblastic anemia and sensorineural deafness.

<i>Staphylococcus aureus</i> alpha toxin

Alpha-toxin, also known as alpha-hemolysin (Hla), is the major cytotoxic agent released by bacterium Staphylococcus aureus and the first identified member of the pore forming beta-barrel toxin family. This toxin consists mostly of beta sheets (68%) with only about 10% alpha helices. The hly gene on the S. aureus chromosome encodes the 293 residue protein monomer, which forms heptameric units on the cellular membrane to form a complete beta barrel pore. This structure allows the toxin to perform its major function, development of pores in the cellular membrane, eventually causing cell death.

Jeremy Randall Knowles was a professor of chemistry at Harvard University who served as dean of the Harvard University faculty of arts and sciences (FAS) from 1991 to 2002. He joined Harvard in 1974, received many awards for his research, and remained at Harvard until his death, leaving the faculty for a decade to serve as Dean. Knowles died on 3 April 2008 at his home.

<span class="mw-page-title-main">Synthetic ion channels</span>

Synthetic ion channels are de novo chemical compounds that insert into lipid bilayers, form pores, and allow ions to flow from one side to the other. They are man-made analogues of natural ion channels, and are thus also known as artificial ion channels. Compared to biological channels, they usually allow fluxes of similar magnitude but are

  1. minuscule in size,
  2. diverse in molecular architecture, and
  3. may rely on diverse supramolecular interactions to pre-form the active, conducting structures.
<span class="mw-page-title-main">Ammonia transporter</span>

Ammonia transporters are structurally related membrane transport proteins called Amt proteins in bacteria and plants, methylammonium/ammonium permeases (MEPs) in yeast, or Rhesus (Rh) proteins in chordates. In humans, the RhAG, RhBG, and RhCG Rhesus proteins constitute solute carrier family 42 whilst RhD and RhCE form the Rh blood group system. The three-dimensional structure of the ammonia transport protein AmtB from Escherichia coli has been determined by x-ray crystallography revealing a hydrophobic ammonia channel. The human RhCG ammonia transporter was found to have a similar ammonia-conducting channel structure. It was proposed that the erythrocyte Rh complex is a heterotrimer of RhAG, RhD, and RhCE subunits in which RhD and RhCE might play roles in anchoring the ammonia-conducting RhAG subunit to the cytoskeleton. Based on reconstitution experiments, purified RhCG subunits alone can function to transport ammonia. RhCG is required for normal acid excretion by the mouse kidney and epididymis.

<span class="mw-page-title-main">KcsA potassium channel</span> Prokaryotic potassium ion channel

KcsA (K channel of streptomyces A) is a prokaryotic potassium channel from the soil bacterium Streptomyces lividans that has been studied extensively in ion channel research. The pH activated protein possesses two transmembrane segments and a highly selective pore region, responsible for the gating and shuttling of K+ ions out of the cell. The amino acid sequence found in the selectivity filter of KcsA is highly conserved among both prokaryotic and eukaryotic K+ voltage channels; as a result, research on KcsA has provided important structural and mechanistic insight on the molecular basis for K+ ion selection and conduction. As one of the most studied ion channels to this day, KcsA is a template for research on K+ channel function and its elucidated structure underlies computational modeling of channel dynamics for both prokaryotic and eukaryotic species.

Oxford Nanopore Technologies plc is a UK-based company which develops and sells nanopore sequencing products for the direct, electronic analysis of single molecules. It is listed on the London Stock Exchange and is a constituent of the FTSE 250 Index.

<span class="mw-page-title-main">Gideon Davies</span> Professor of Chemistry

Gideon John Davies is a professor of chemistry in the Structural Biology Laboratory (YSBL) at the University of York, UK. Davies is best known for his ground-breaking studies into carbohydrate-active enzymes, notably analysing the conformational and mechanistic basis for catalysis and applying this for societal benefit. In 2016 Davies was appointed the Royal Society Ken Murray Research Professor at the University of York. Gideon Davies has recently been elected to the Council of the Royal Society.

<span class="mw-page-title-main">Cytotoxin K</span> This protein is one of the toxins excreted by bacillus cereus and causes abdominal symptoms

Cytotoxin-K (CytK) is a protein toxin produced by the gram-positive bacteria Bacillus cereus. It was first discovered in a certain Bacillus cereus strain which was isolated from a food poisoning epidemic that occurred in a French nursing home in 1998. There were six cases of bloody diarrhea, three of which were fatal. None of the known enterotoxins from B. cereus could be detected at this time. Later, this B. cereus strain and its relatives were classified as a brand-new species called Bacillus cytotoxicus, which is the thermo-tolerant member of the B. cereus genus. The cytotoxin-K gene is present in approximately 50% of Bacillus cereus isolates, and its expression is regulated by several factors, including temperature and nutrient availability.

References

  1. 1 2 3 4 "BAYLEY, Prof. (John) Hagan (Pryce)" . Who's Who . Vol. 2014 (online edition via Oxford University Press  ed.). A & C Black.(Subscription or UK public library membership required.)
  2. ↑ Branton, D.; Deamer, D. W.; Marziali, A.; Bayley, H.; Benner, S. A.; Butler, T.; Di Ventra, M.; Garaj, S.; Hibbs, A.; Huang, X.; Jovanovich, S. B.; Krstic, P. S.; Lindsay, S.; Ling, X. S.; Mastrangelo, C. H.; Meller, A.; Oliver, J. S.; Pershin, Y. V.; Ramsey, J. M.; Riehn, R.; Soni, G. V.; Tabard-Cossa, V.; Wanunu, M.; Wiggin, M.; Schloss, J. A. (2008). "The potential and challenges of nanopore sequencing". Nature Biotechnology. 26 (10): 1146–1153. doi:10.1038/nbt.1495. PMC   2683588 . PMID   18846088.
  3. 1 2 3 "Hagan Bayley". The Royal Society.
  4. 1 2 3 4 "CURRICULUM VITAE Hagan Bayley" (PDF). Retrieved 26 February 2018.
  5. ↑ http://bayley.chem.ox.ac.uk/ Bayley group at the University of Oxford
  6. ↑ http://research.chem.ox.ac.uk/hagan-bayley.aspx Archived 26 April 2011 at the Wayback Machine Hagan Bayley Research page
  7. ↑ Hagan Bayley's publications indexed by the Scopus bibliographic database. (subscription required)
  8. ↑ Braha, O.; Braha, H.; Conlan, L. Q.; Cheley, S.; Bayley, S. (1999). "Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter". Nature. 398 (6729): 686–690. Bibcode:1999Natur.398..686G. doi:10.1038/19491. PMID   10227291. S2CID   4366779.
  9. ↑ Lou, H; Chen, M; Black, S. S.; Bushell, S. R.; Ceccarelli, M; Mach, T; Beis, K; Low, A. S.; Bamford, V. A.; Booth, I. R.; Bayley, H; Naismith, J. H. (2011). "Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. Coli". PLOS ONE. 6 (10): e25825. Bibcode:2011PLoSO...625825L. doi: 10.1371/journal.pone.0025825 . PMC   3203869 . PMID   22053181.
  10. ↑ Balliol College Register (Fifth ed.). 1983. p. 457.
  11. ↑ Bayley, Hagan (1979). Adamantylidene: A Hydrophobic, Photogenerated Reagent for the Characterization of Intrinsic Membrane Proteins (PhD thesis). Harvard University. ProQuest   302912373.
  12. ↑ Bayley2009-05-29T18:07:20+01:00, Hagan. "Nanopores for thought". Chemistry World. Retrieved 22 January 2021.{{cite web}}: CS1 maint: numeric names: authors list (link)
  13. ↑ Howorka, S.; Cheley, S.; Bayley, H. (2001). "Sequence-specific detection of individual DNA strands using engineered nanopores". Nature Biotechnology. 19 (7): 636–639. doi:10.1038/90236. PMID   11433274. S2CID   447980.
  14. ↑ Bayley, Hagan Profile at the University of Oxford Archived 17 January 2010 at the Wayback Machine
  15. ↑ Song, L.; Hobaugh, M. R.; Shustak, C.; Cheley, S.; Bayley, H.; Gouaux, J. E. (1996). "Structure of Staphylococcal alpha -Hemolysin, a Heptameric Transmembrane Pore". Science. 274 (5294): 1859–1865. Bibcode:1996Sci...274.1859S. doi:10.1126/science.274.5294.1859. PMID   8943190. S2CID   45663016.
  16. ↑ Hagan Bayley publications indexed by Google Scholar
  17. ↑ Bayley, Hagan Profile at Hertford College
  18. ↑ Wales, The Learned Society of. "Hagan Bayley". The Learned Society of Wales. Retrieved 22 August 2023.
  19. ↑ "The UK's 100 leading practising scientists". 17 January 2014.


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