SOME previously  FILLED/Advertized  positions

Details of new PhD or postdoctoral opportunities will be posted here.

Potential PhD applicants with a 2.1 or First in Chemistry or equivalent (eg M.Sc./M.Phil) are always welcome, and should send a CV by email. Informal enquiries welcome.

Applications are invited for PhD research projects.  Informal enquiries are welcome via email (Click’email’ to creat an email).

BBSRC-funded PhD Studentship

This project will contribute to investigating the structure-activity relationships of carbohydrate molecules targeted at a growth factor. The work will involve synthesis of saccharide molecules and in their evaluation in biological assays. The project is multi-disciplinary and you will be trained in both bioactive carbohydrate synthettic chemistry and in running biological evaluations, with assistance from chemistry and biology postdocs also working on the programme.

The project will be of interest if you are wanting to be involved in biological synthetic chemistry, but also would like to be trained in biological screening methods and analysis. The biological work will be done in new labs at the Paterson Institute in Manchester in collaboration with Prof Gordon Jayson. Your will be based in the School of Chemistry and work in the new Manchester Interdisciplinary Biocentre building. You will join a chemistry research group with several postdocs in biocatalysis-related synthesis and carbohydrate/oligosaccharide synthesis, and several other PhD students. For more information visit our web site.

For an application form, please email: or complete an online application form using the following web link



SCHOOL OF CHEMISTRY and Manchester Interdisciplinary Biocentre

BBSRC Postdoctoral Research Associate in Synthetic Chemistry and Biocatalysis 

This 5-year BBSRC-funded Chemistry position is part of a multi-disciplinary collaboration involving synthetic chemistry and biocatalysis, enzymology and microreactor engineering (Drs Gardiner and Stephens,Profs Scrutton, Munro and Dr Leys and Profs Goddard and Fielden). The overall aim is to develop a viable manufacturing process to exploit a wide range of novel and industrially relevant redox biotransformations using microfabricated reactors for the production of high value chiral products. This post will involve a range of synthesis, including arrays, biocatalysis and evaluation and analysis of biocatalytic processes. The work will be based in the new Manchester Interdisciplinary Biocentre ( and this position will give you an exciting opportunity to work in a large inter-disciplinary team in new state-of-the-art facilities. You will join a chemistry research group with several other PDRAs and activity in synthetic biologically-targeted chemistry. More information is available via the MIB web site about the research groups collaborating in this programme.

Applicants should have a PhD in Synthetic Chemistry/Biocatalysis or related subject. Experience of chemical synthesis (and the ability to design and plan new syntheses). Some and analytical chemistry (especially chiral analysis) is essential and experience of work in biocatalyst discovery/development projects would be a significant advantage.  experience of biocatalysis using whole cells and/or isolated enzymes and use of multiphase reactions would be beneficial. Informal enquiries are welcome to

Application forms and further particulars are available from our website

If you are unable to go online you can request a hard copy of the details from The Directorate of Human Resources, Faculty of Engineering and Physical Sciences, Tel: +44 (0) 161 275 8837, email:

Closing date: 28 February 2007.  Please quote reference EPS/023/07

The University will actively foster a culture of inclusion and diversity and will seek to achieve true equality of opportunity for all members of its community..

University of Manchester

Manchester Interdisciplinary Biocentre

PhD Studentship - Biocatalytic amide reduction | Closing date: 11th July 2008

Applications are invited for an industrially-funded PhD studentship on biocatalytic reduction of amides, in the UK Centre of Excellence for Biocatalysis (CoEBio3; see Reduction of amides to amines is a new type of enzymatic reaction, demonstrated for the first time in our research group. In addition to the fundamental scientific interest in this new reaction, the enzyme could be extremely useful for industrial biotransformations, since biocatalytic amide reduction offers a mild, selective, environmentally benign alternative to the equivalent, rather problematic chemical reduction. Therefore, this new biotransformation will be extremely useful in industry to synthesize complex amines for manufacturing pharmaceuticals and other speciality chemicals.  In this project, you will purify and characterise the amide reductase, clone the corresponding gene(s) and test the enzyme for industrially useful biotransformations.  You will, therefore, develop skills in enzymology, protein purification, and molecular biology, and you will also learn how to run biotransformations.  You will work in the new Manchester Interdisciplinary Biocentre (, a new, state-of-the-art building for research in Interdisciplinary Bioscience which has excellent facilities for biocatalysis research. The project will be co-supervised by Drs Gill Stephens


and John Gardiner

(see You will join a thriving research group, funded by BBSRC, TSB and industry, and including a number of other postdocs and students working on closely related projects.  Your degree should be in biochemistry, microbiology, biological chemistry or a related discipline (minimum 2.1 honours, MSc or equivalent).  Eligibility for full funding is restricted to UK or EU citizens, with the stipend at the standard EPSRC rate.  The project will start in October 2008.

Please apply by sending your CV, a brief statement of your research interests, and the names and email addresses of two referees to Dr Gill Stephens, to whom informal enquiries may also be made.  Email:  Address: Dr Gill Stephens, Manchester Interdisciplinary Biocentre, University of Manchester, 131 Princess Street, Manchester M1 7DN.

Postdoctoral Research Associate in Synthetic/Biomedical Carbohydrate Chemistry



Applications are invited for a postdoctoral position to contribute to synthesis of carbohydrate (oligosaccharide) targets as potential antitumour agents. This work is a CRUK-funded collaboration between University of Manchester, School of Chemistry and the Department of Medical Oncology (Paterson Institute/Christie Hospital).  The work will involve synthesis of carbohydrate intermediates and oligosaccharides and provision of samples for biological evaluation at the Paterson Institute. The successful applicant will be part of a closely collaborating team involving organic synthesis, molecular biology and preclinical drug development.

Applicants will require a PhD in synthetic or bioorganic chemistry and experience in carboyhydrate-related work would be highly desirable. Informal enquiries welcome to Dr John Gardiner (+44 (0)161 306 4530; email Dr Gordon Jayson (+44 (0)161 446 3606; email The appointment is available for one year initially.

Application forms and further particulars are available from our website If you are unable to go online you can request a hard copy of the details from The Directorate of Human Resources, Faculty of Engineering and Physical Sciences, Tel: +44 (0) 161 275 8837, email:  Please quote reference MHS/90510 and submit applications, by mail or email, to Human Resources and copy to PIs. April 30, 2009. Salary will be within the University Grade 6 range according to relevant experience and qualifications.

Frances and Barrie Bernstein Research Fellowship

Synthetic Carbohydrate Chemistry / Biological Chemistry

School of Cancer & Enabling Sciences & 

School of Chemistry / Manchester Interdisciplinary Biocentre

Closing date: 24/03/2011

Reference: EPS/11741

This project is developing synthesis of oligosaccharide targets with promising activity as potential antitumour agents, and their evaluation as antagonists of fibroblast growth factor (FGF)-mediated angiogenesis and pursuing insights into structure-activity roles. The work is a collaboration between Manchester School of Chemistry and the University of Manchester Department of Medical Oncology and will be based in the Manchester School of Chemistry. This post will involve developing methods, and carrying out target carbohydrate and oligosaccharide syntheses, and so will involve a variety of synthetic carbohydrate chemistry, on a range of scales.

You will work within a closely inter-disciplinary team of current researchers in both chemistry and biology on this project, and so synthetic work will involve close collaboration with others at postdoctoral and graduate student levels, in both disciplines. Materials you will be involve din preparing will be evaluated in biological assays within the team, providing an exciting environment of synthesis and rapid biological feedback to synthesis design. You will need to be able to make a significant contribution in collaborating on carrying out oligosaccharide syntheses within the first 6-9 months. Therefore you must hold or be about to obtain a PhD or equivalent in synthetic chemistry, preferably with carbohydrate experience, together with excellent communication, organisational & team working skills.

The post is available immediately and is tenable for up to 18 months.


£29,099 - £35,788 p.a.

Informal enquiries

Dr John Gardiner

Tel: + 44 (0) 161 306 4530 



Prof Gordon Jayson

Tel: +44 (0)161 446 3606


For further particulars and an application form please visit:

Synthesis and New Applications of Labelled, Biologically Important Saccharides.

Oligosaccharides are ubiquitous biomolecules on cell surfaces, and many biological recognition processes involve key roles for such carbohydrate structures, including many host cell recognition events (e.g. embryogenesis), various cancer-related processes (e.g. metastasis, mediation of angiogenesis) as well as being common to many pathogen (bacterial, viral) attachment processes critical to infectivity. Understanding carbohydrate-mediated interactions, most particularly with the protein receptors to which they bind, is at the forefront of chemical biology. A key arena for future discovery is developing methods to be able to probe the structure of saccharides in solution, and also where and how they bind. Attaching spectroscopic labels to saccharides can provide a unique handle to be able to detect and track the behaviour and locations of biological saccharides. This project will build on synthetic expertise in providing biologically-relevant synthetic saccharides which has provided several saccharides with in vivo biomedical efficacy and exploit this to develop synthesis and applications of new labeled saccharides. These high value new tools for glycol-chemical biology will be used to probe structure and follow biological effects in vitro and in vivo. This work will be highly multidisciplinary within the School of Chemistry, with training in synthesis and spectroscopy.

Collaboration: This project is part of a wider programme involve synthetic methods for carbohydrate and oligosacccharide synthesis, and the application of these towards new tools for glycobiology chemical biology. This PhD project will be taking forwards our development of new saccharide tools to use to probe the structure and binding of biological important saccharides.

Industrial biocatalysis: chemoenzymatic routes to non-steroidal anti-inflammatory 2-aryl propionic acids (profens).

Prof Nigel Scrutton, Dr John Gardiner and Prof David Leys

Industrial biotechnology in chemicals manufacture is one of the key enabling technologies in the 21st Century. The European chemical industry is the largest in the world and biotechnology is poised to make a substantial impact on chemicals production. The manufacture of chiral molecules is a particular challenge. In this research we will develop new biocatalysts to synthesise enantiopure versions of the globally most widely used analgesic compounds used in human and animal medicine. This will impact widely on available technologies for profen analgesic manufacture by providing innovative and competitive green solutions to their manufacture that avoid problems with landfill, toxicity and supply in current manufacturing processes.

Current manufacturing methods generate the profen racemates. New enzymatic methods could produce biologically active profen (S)-enantiomers. This has clear advantages in terms of reduction in total administered dose, enhanced therapeutic window, minimisation of side effects and more precise pharmacokinetic properties. Research will involve determination of structures of target enzymes, biotransformation studies of chemical conversions using synthesised substrates, and directed/focused evolution of target enzymes to obtain improved catalytic properties with target substrates. We will focus on oxidoreductases and related enzyme systems for which we have demonstrated desirable catalytic properties in work supporting this project. The project is founded on (i) a strong knowledge base from our previous mechanistic and biocatalytic studies of this class of enzyme, (ii) our supporting synthetic work, (iii) a demonstrated ability to evolve enzymes in this enzyme class and (iv) a strong partnership with industrial partners motivated to exploit oxidoreductases in industrial environments.

Collaboration: This project is a multidisciplinary collaboration in particular with Prof Nigel Scrutton’s enzymology group, one of the UK’s leading biocatalysis/enzymology labs, based in the MIB, and also in collaboration with David Leys enzyme structural biology group. This forms part of a wider collaboration between our groups and you would thus not only gain extensive synthetic training and experience but interact with world-leading biocatalysis/enzymology within the MIB.

Application of isotope-discriminated NMR to understanding of the interaction of structurally-defined synthetic heparin sulphate oligosaccharides with FGF-FGFR

Principal Supervisor: Dr John Gardiner (Chemistry), Co-Supervisors: Dr Alexander Golovanov (FLS, MIB) and Prof Gordon Jayson (Paterson Institute).

Heparan sulfate (HS) oligosaccharides play important regulatory roles in a number of biological processes, including regulation of growth factors (eg Fibroblast Growth Factors (FGFs)) which have an obligate dependency on HS ligands), and play roles in development and morphogenesis, and are involved in various disease states, such as cancer. For example, these interactions are involved in processes such as angiogenesis, critical to the growth of blood vessels in many tumours, and thus understanding and ultimately inhibiting this with synthetic ligands, could offer new therapeutic applications. Whilst there have been studies of interactions of some HS structures with FGFs utilizing crystallography and NMR of HS-FGF complexes, there is considerable current importance in understanding the interactions of discrete HS ligands with the FGF-FGFR complex, to probe the definitive structural aspects relating to ligand selectivities. This project will involve using pure HS species with defined structural modifications as tools to combine with powerful new isotope-discriminating NMR methods to be able to probe and determine the binding structures of structurally-specific HS ligands with the ternary complex (HS-FGF-FGF2) which is the biological effector of HS-triggered signalling.

Collaboration: This project is a multidisciplinary collaboration and part of a wider project in which we have developed new, scalable synthesis of a range of bioactive carbohydrates. This project will involve you interacting with synthetic carbohydrate expertise and learning techniques in NMR applied to protein-carbohydrate interactions, providing interdisciplinary training at the forefront of new chemical structural biology applications. 

Expanding the toolkit for biocatalytic hyrdogenations: 3 year PhD Studentship funded by the Centre of Excellence in Biocatalysis, Biotransformations and Biocatalytic Manufacture. AVAILABLE FOR SEPT/OCT 2013 START

Prof Nigel Scrutton, Dr John Gardiner

Biocatalytic hydrogenations of a,b-unsaturated compounds are traditionally performed by a variety of ‘ene’-reductases, belonging to the Old Yellow Enzyme (OYE) family. These FMN-containing oxidoreductases catalyse the NAD(P)H-dependent activated alkene reduction of a variety of a,b-unsaturated aldehydes, ketones, nitroalkenes, nitriles, steroids and dicarboxylic acids.e.g.1 OYEs have been isolated from many yeast and bacterial species, and extensive in vitro and in vivo studies have shown their general applicability in biocatalytic hydrogenations. However, the substrate specificity of these enzymes tends to be limited to mostly small molecules, with some classes of compounds poorly reduced (e.g. alkenes containing monocarboxylic acid activating groups).1 In addition, the reaction rate and sometimes the product enantiopurity are affected by the presence of oxygen, due to the presence of an FMN cofactor.

The program will extend hydrogenation of a,b-unsaturated compounds to a new class of biocatalyst currently under represented in the biocatalysis tool box. It is likely to generate biocatalysts with very different reactivity profiles which may be difficult to find through conventional directed evolution programs using OYEs. This new class of biocatalyst would be more robust for exploitation under aerobic conditions, since the enantioselectivity and reactivity of OYE biocatalysts is potentially variable under aerobic/anaerobic conditions.2

The student will receive training in relevant science related to biocatalysis. This will involve training in analytical chemistry, enzymology, biotransformations, small molecule synthesis, recombinant DNA methodologies, protein purification, modelling and structural biology. The student will join a vibrant and large group working in the area of biocatalysis, enzyme structure and mechanisms, which is well funded and supported by senior postdoctorals and EOs. The student will therefore get wide exposure to contemporary biocatalysis/enzymology research through his/her interactions in the group and the wider biocatalysis groups on the 2/3 floors of MIB.

Collaboration: This project is a multidisciplinary collaboration in particular with Prof Nigel Scrutton’s enzymology group, one of the UK’s leading biocatalysis/enzymology labs, based in the MIB. This forms part of a wider collaboration between our groups funding by a BBSRC synthetic biology program, and you would thus gain extensive synthetic training and experience with world-leading biocatalysis/enzymology within the MIB.

Postdoctoral Research Associate in Biocatalysis and Synthetic Biology

Prof Nigel Scrutton, Dr John Gardiner                                                                                    AVAILABLE FOR NOV/DEC 2013 START

Applications are invited for a postdoctoral position to contribute to a BBSRC-funded / GSK-supported multidisciplinary programme which is aiming to develop synthetic production of monoterpenoids which are found in a wide range of industrially important flavours and medicinal compounds. This programme is developing a synthetic biology programme engineering artificial pathways for monoterpenoids based on knowledge of the activities and structures of component enzymes (or their variants) that display desired catalytic properties. Our programme thus integrates synthetic biology, systems-based approaches, with biocatalysis and analysis of enzyme structures and mechanisms. A key part of this programme is the synthesis of various terpenoid substrates, both native, analogues and also biosynthetic intermediates, allied with developing methods for characterization of new biocatalytic products and exploring/developing useful new biocatalytic applications of terpenoid-transforming enzymes. The appointee will thus have scope for synthetic chemistry combined with experience in applying bioacatalysis and will work in both synthetic chemistry and enzymology/biocatalysis labs in the Scrutton and Gardiner groups in MIB. The appointee will join a vibrant and large group working in the area of biocatalysis for high value target synthesis, and enzyme structure and mechanisms.

Applicants will require a PhD in synthetic/bioorganic chemistry/chemical biology or biocatalysis and must have experience in synthetic work and associated analytical methods. Experience of biocatalysis and use of HPLC / GC-MS would be an advantage. The appointee should be able to work independently but also will be a part of a closely interacting inter-disciplinary project group of other PDRAs and research students in synthesis, enzymology and biocalalysis and evidence of managing research students would be an advantage. The multi-disciplinary nature of the programme and the need to regularly present results to our GSK collaborators mean excellent communication skills are essential.

Informal enquiries are very welcome to Dr John Gardiner (+44 (0)161 306 4530; email or Prof Nigel Scrutton (+44 (0)161 306 5152; email

The appointment is made for one year in the first instance with funding available for up to 33 months to Summer 2016.

Collaboration: This project is a multidisciplinary collaboration with Prof Nigel Scrutton’s enzymology group, one of the UK’s leading biocatalysis/enzymology labs, based in the MIB. This forms part of a wider collaboration between our groups funding by a BBSRC synthetic biology program, and you would thus gain extensive synthetic training and experience with world-leading biocatalysis/enzymology within the MIB.


PhD studentships are available for Sept 2017 in areas of carbohydrate synthesis/ medicinal chemistry and chemical biology. See also on

Applications open for BBSRC and MRC PhD Studentships in Carbohydrate Synthesis, New Tools for Chemical Biology and Medicinal Chemistry for PhDs starting Sept 2017. Application deadline Nov 18, 2016.

Two PhDs are currently open for applications. Informal enquiries for further information are very welcome.

BBSRC: Oligosaccharides are ubiquitous biomolecules on cell surfaces and the intra-cellular matrix, and are central to many critical biological regulatory processes, including cell-differentiation, cancer, bacterial and viral infections and inflammation. In particular, heparan sulphate oligosaccharides (HSOs) are essential to many such processes, so there is major interest in advancing our understanding of HS chemical biology and biomolecular interactions. A better understanding of the area will lead to new technologies that exploit carbohydrate structures for the development of related next-generation glycotherapeutics. Liposomal drug development is of interest because it allows delivery of potentially toxic drugs in a sustained manner to tumours, while reducing toxicity to non-target organs.

This project involves an exciting multidisciplinary combination of synthetic carbohydrate and oligosaccharide chemistry and liposome technology to develop a platform with potential across a number of biomedical targets. The project requires working in a multidisciplinary team to build on technologies and IP developed at the University of Manchester. The synthesis of pure synthetic HSO-fragments and modified derivatives will be combined with forefront work on biomolecule-modified liposomes (see references) and cell biological efficacy at the Manchester Cancer Research Centre. This work will be conducted in two groups both based in the Manchester Institute of Biotechnology / School of Chemistry (Gardiner/Webb) and biological work will be undertaken in the Manchester Cancer Research Centre (Jayson lab), a new state-of-the-art research centre opened in 2016.

• Jayson, G. C.; Gardiner, J. M. et al Nature Commun. 2013, DOI: 10.1038/ncomms3016.

• Miller, G. J.; Jayson, G. C.; Gardiner, J. M. et al Chemical Science 2013, 4, 3218-3222.

• Coxon, T. P.; Fallows, T. W.; Gough, J. E.; Webb, S. J. Org. Biomol. Chem. 2015, 13, 10751–10761.

• Poli, M.; Zawodny, W.; Quinonero, O.; Lorch, M.; WebbS. J.; Clayden, J. Science, 2016, 352, 575-580.

Both projects will provide a wide range of synthetic training and experience alongside multidisciplinary training and collaborations with, and in, other research groups providing interdisciplinary training at the forefront of new chemical structural biology applications. 

MRC: : Antimicrobial resistance (AMR) has become a global crisis threatening our health care system and causing huge economic loss.  Currently MRSA strains are resistant to nearly all beta-lactam antibiotics, leaving few options for treatment of MRSA infections due to emerging MRSA strains with resistance to ‘last resort ‘antibiotics. There is thus urgent need to study the novel resistance mechanisms of MRSA and develop novel diagnostics and antibiotics to combat MRSA infection. Most gram positive bacteria are densely decorated with wall teichoic acids (WTAs), which play critical roles in cell division, biofilm formation, and interactions with host cells and bacteriophages.1-3 Wall teichoic acids are composed of repetitive ribitotolphosphate (RboP) connected via 1,5 phosphodiester bonds, and anchired to the cell wall via disaccharide carbohydrate units, and the nature and sites of additional glyosylations plays a  roles in bacteria drug resistance. A few  WTA interaction proteins have been identified and characterized, however, lack of pure WTA oligomers with defined substitutions/length greatly hinders investigation of WTA interactions. This project will develop a new approach to generate diverse, pure, site-programmable WTA fragments, which provide powerful tools to probe the biology of WTA interactions and thereby underpin the potential development of approaches to novel diagnostics and antibiotics. The project will involve collaboration between the carbohydrate synthetic expertize of the Gardiner group and biomedical WTA expertize of the Xia lab in the School of Medicine, utilizing recent crystal structure work.

Example relevant work:

1. Winstel V, Xia G*, Peschel A. Int. J. Med. Microbiol, (2014), 304(3-4):215-221

2. Brown S, Xia G*, Walker S* et al  Proc. Natl. Acad. Sci. USA (2012), 109: 18909-14.

3. Li X , Koc C, Kuener P, Stierhof Y, Enright MC, Penades JR, Wolz C, Stehle T, Cambillau C,Peschel A, Xia G. Sci Rep (2016), 6, [26455].

4. Gardiner JM et al. J. Org. Chem. (2015), 80, 3777-3789.

5. Jayson GC, Gardiner JM et al. Chemical Science (2013), 4: 3218-3222.

6. Jayson GC, Gardiner JM et al Nature Commun. (2013), DOI: 10.1038/ncomms3016.