Prof. David Phoenix OBE

Prof. David Phoenix

Vice-Chancellor

  • Telephone:
    020 7815 6018
  • Professional service:
    Executive
 

Professor David Andrew Phoenix, OBE, DL, DUniv, AcSS, DSc is the Vice Chancellor of London South Bank University, Chair of millionPlus, and a member of the HEFCE Strategic Committee for Teaching Quality and the Student Experience. He was elected to Fellowship of the Royal College of Physicians (Edinburgh) for his contribution to medical research and education and recognized as an Academician by the Academy of Social Sciences for his work in areas linked to educational policy. He currently represents Universities UK on the UK Performance Indicator Steering Group.

In 2015 the Prime Minister appointed him as a trustee of the Science Museum Group. He is also a trustee of Universities UK and a Director of the National Centre for Universities and Business.

With over 250 publications, Prof. Phoenix remains a visiting professor at Kings College London and Sichuan University, China, as well as a Fellow of the Royal Society of Chemistry, The Society of Biology, The Institute of Mathematics and Its Applications, and the Royal Society of Medicine. Through these later bodies he has engaged in a range of discussions regarding the skills agenda, especially related to employer requirements. In 2010 he was made an Officer of the Most Excellent Order of the British Empire for services to Science and Higher Education, and appointed as a Deputy Lieutenant of Greater London in 2015.

Prof. Phoenix has worked extensively overseas, developing and leading on an overseas campus in Cyprus and a research institute in China. He was awarded an individual Excellence award by China’s Vice Premier in 2014 and was admitted to Order of Friendship (China) in 2016 for outstanding contribution to the country’s economic and social development.

Dave's research is multidisciplinary and draws on a range of specialisms including, biology, chemistry, engineering, physics and computational modelling to help develop understanding of the structure function relationships used by amphiphilic bioactive molecules. The term ‘‘peptide-amphiphile’’ can be used to describe amphiphilic peptides consisting only of amino acids that show segregation of charged and uncharged components within the primary or secondary structure. Alternatively they may be composed of hydrophilic peptides linked to hydrophobic alkyl chains or lipids, and peptide based copolymers. Such molecules are of significant biological importance due to the range of asymmetric boundaries that occur in nature such as those found at a membrane lipid interface. Amphiphilic protein sequences can be involved in protein targeting, membrane protein assembly as well as membrane fusion and lysis. In addition to amphiphilic peptides possessing key biological functions amphiphiles are becoming of increasing interest in the creation of new biomaterials. Amphiphiles can self-assemble into a variety of different structures such as micelles, vesicles, monolayers, bilayers, nanofibers, nanotapes, ribbons, and twisted ribbons, to minimise unfavorable interactions with their surroundings. A key aspect of his work involves the development of bioactive peptides and new biomaterials with biomedical application.

Most recent publications

Dennison, SR and Harris, F and Phoenix, DA Investigations into the potential anticancer activity of Maximin H5. Biochimie, 137. 29-34. DOI 10.1016/j.biochi.2017.02.013

Najlah, M and Jain, M and Wan, KW and Ahmed, W and Albed Alhnan, M and Phoenix, DA and Taylor, KMG and Elhissi, A Ethanol-based proliposome delivery systems of paclitaxel for in vitro application against brain cancer cells. Journal of Liposome Research, 1-12. DOI 10.1080/08982104.2016.1259628

Malik, E and Dennison, SR and Harris, F and Phoenix, DA PH dependent antimicrobial peptides and proteins, their mechanisms of action and potential as therapeutic agents. Pharmaceuticals, 9. DOI 10.3390/ph9040067

Dennison, S and Morton, L and Harris, F and Phoenix, DA Low pH enhances the action of maximin H5 against Staphylococcus aureus and helps mediate lysylated phosphatidylglycerol induced resistance. Biochemistry, 55. 3735-3751. DOI 10.1021/acs.biochem.6b00101

Mura, M and Wang, J and Zhou, Y and Pinna, M and Zvelindovsky, AV and Dennison, SR and Phoenix, DA The effect of amidation on the behaviour of antimicrobial peptides. European Biophysics Journal, 45. 195-207. DOI 10.1007/s00249-015-1094-x

Phoenix, DA and Dennison, SR and Harris, F Bacterial resistance to host defence peptides. In: Host Defense Peptides and Their Potential as Therapeutic Agents. Springer International Publishing, pp. 161-204. ISBN 9783319329499 DOI 10.1007/978-3-319-32949-9_7

Famlia, C and Dennison, SR and Quintas, A and Phoenix, DA Prediction of Peptide and Protein Propensity for Amyloid Formation. Plos One, 10. DOI 10.1371/journal.pone.0134679

Dennison, SR and Mura, M and Harris, F and Morton, LH and Zvelindovsky, A and Phoenix, DA The role of C-terminal amidation in the membrane interactions of the anionic antimicrobial peptide, maximin H5.. Biochim Biophys Acta, 1848. 1111 - 1118. DOI 10.1016/j.bbamem.2015.01.014

More publications at LSBU Research Open
  • Principal Fellow, Higher Education Academy
  • Fellow and Chartered Chemist, Royal Society Chemistry,
  • Fellow and chartered biologist, Royal Society  of Biology
  • Fellow, Royal Society Medicine
  • Fellow and chartered mathematician, Institute of Mathematics and its Applications, (FIMA)
  • Prime Ministerial appointment as a Trustee Science Museum Group, Chair of Audit Committee and a member of the Museum of Science and Industry Advisory Board
  • Trustee, British University in Egypt
  • Director, National Centre for Universities and Business
  • Chair of Millionplus – the association of modern universities
  • Member of the Minister for Universities and Science Brexit advisory Forum
  • Inaugural Chair South Bank Academies
 
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