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">M2 proton channel</span>

The Matrix-2 (M2) protein is a proton-selective viroporin, integral in the viral envelope of the influenza A virus. The channel itself is a homotetramer, where the units are helices stabilized by two disulfide bonds, and is activated by low pH. The M2 protein is encoded on the seventh RNA segment together with the M1 protein. Proton conductance by the M2 protein in influenza A is essential for viral replication.

The Transporter Classification Database is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins, including ion channels.

<span class="mw-page-title-main">P2X purinoreceptor</span>

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.

Light-gated ion channels are a family of ion channels regulated by electromagnetic radiation. Other gating mechanisms for ion channels include voltage-gated ion channels, ligand-gated ion channels, mechanosensitive ion channels, and temperature-gated ion channels. Most light-gated ion channels have been synthesized in the laboratory for study, although two naturally occurring examples, channelrhodopsin and anion-conducting channelrhodopsin, are currently known. Photoreceptor proteins, which act in a similar manner to light-gated ion channels, are generally classified instead as G protein-coupled receptors.

<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.

Sheena Elizabeth Radford FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics and a Royal Society Research Professor in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds. Radford is the Associate Editor of the Journal of Molecular Biology.

Oxford Nanopore Technologies plc is a UK-based company which develops and sells nanopore sequencing products for the direct, electronic analysis of single molecules.

Pore-C is a genomic technique which utilizes chromatin conformation capture (3C) and Oxford Nanopore Technologies' (ONT) long-read sequencing to characterize three-dimensional (3D) chromatin structure. To characterize concatemers, the originators of Pore-C developed an algorithm to identify alignments that are assigned to a restriction fragment; concatemers with greater than two associated fragments are deemed high order. Pore-C attempts to improve on previous 3C technologies, such as Hi-C and SPRITE, by not requiring DNA amplification prior to sequencing. This technology was developed as a simpler and more easily scalable method of capturing higher-order chromatin structure and mapping regions of chromatin contact. In addition, Pore-C can be used to visualize epigenomic interactions due to the capability of ONT long-read sequencing to detect DNA methylation. Applications of this technology include analysis of combinatorial chromatin interactions, the generation of de novo chromosome scale assemblies, visualization of regions associated with multi-locus histone bodies, and detection and resolution of structural variants.

<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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