Staff profile

Research Interests

Dr John M Sanderson has research interests in Biophysical Chemistry, with a particular emphasis on biological membranes. He is a committee member of the British Biophysical Society, and a member of the Biophysical Society (US) and the Royal Society of Chemistry (MRSC). Research expertise in the group includes amino acid and peptide synthesis, liposome technology and techniques for studying biological membranes, including surface tensiometry, calorimetry, x-ray scattering, optical microscopy and mass spectrometry. Current work is directed towards the study of protein-membrane interactions over all timescales and the preparation of asymmetric lipid membranes for biophysical studies of membrane activity (funded by an EPSRC programme grant).

Membrane-Active Peptides

Work encompasses the design of peptides that have the potential to form stable pores in lipid membranes, the characterisation of peptide interactions with membrane lipids and the physical organic chemistry of peptide reactions in membranes. Particular interests include the kinetics of peptide rearrangements following membrane binding¹ and the chemical stability of peptide-lipid systems. Recent work has begun to establish the factors that control the innate reactivity of peptides towards acyl transfer from membrane lipids (intrinsic lipidation).²

http://community.dur.ac.uk/j.m.sanderson/science/peptides/saps.html

Membrane Protein Chemistry

The behaviour of membrane proteins in membranes is being examined using a range of analytical approaches. Post-translational modifications to aquaporin-0 are being examined by mass spectrometry and reveal a diverse lipidation profile at each of the two lipidation sites of the protein (with Prof. R. A. Quinlan, Biological Sciences, Durham University). The membrane-binding properties of proteins from enveloped viruses are being characterised by a combination of microscopy, chemical biology and structral biology approaches (with Dr R. P. Yeo, Biological Sciences, Durham University). This has led to the structure determination for RSV M protein (in collaboration with Dr V. Money),³ and studies of membrane bindign using tensiometry, electron microscopy, circular dichroism and Brewster angle microscopy.⁴

http://community.dur.ac.uk/j.m.sanderson/science/virus/rsv.html

Amino Acid and Drug-Lipid Interactions

We have used host-guest chemistry⁵ to test the hypothesis that aromatic amino acids have thermodynamically significant interactions with the headgroups of neutral lipids such as phosphatidylcholines. In the case of the Tryptophan and Tyrosine, we have demonstrated that both preferentially form 2:1 adducts with lipids. Using NMR and modelling approaches, we have been able to rationalise the adducts formed between Tryptophan and phosphocholine headgroups in terms of the intermolecular interactions involved. Current work is examining the chemistry exhibited by drug molecules after their adsorbtion to lipid membranes.

http://community.dur.ac.uk/j.m.sanderson/science/peptide_lipid/pl.html

Spectroscopy and Microscopy of Lipid Membranes

Current work centres around the synthesis and exploitation of labelled lipids and sterols.⁶ In previous work we demonstrated the generation of Raman spectra from individual trapped liposomes and the use of Scanning Electrochemical Microscopy (SECM) to observe redox switching of a modified gramicidin channel (with Dr R. Kataky, Durham University). Brewster angle microscopy has been used to characterise the association of peripheral membrane proteins with lipid monolayers (with Dr A Beeby, Durham University).⁴

http://community.dur.ac.uk/j.m.sanderson/science/membranes/lipid.html

References

1. Catherine J. Pridmore, Alison Rodger and John M. Sanderson, Biochim. Biophys. Acta, 2016, 1858, 892–903.
2. Robert H. Dods, Burkhard Bechinger, Jackie A. Mosely and John M. Sanderson, J. Mol. Biol., 2013, 425, 4379–4387.
3. Victoria A. Money, Helen K. McPhee, Jackie A. Mosely, John M. Sanderson and Robert P. Yeo, Proc. Natl. Acad. Sci. U. S. A., 2009, 106, 4441–4446.
4. Helen K. McPhee, Jennifer L. Carlisle, Andrew Beeby, Victoria A. Money, Scott M. D. Watson, Robert P. Yeo and John M. Sanderson, Langmuir, 2011, 27, 304–311.
5. Georg Blaser, John M. Sanderson and Mark R. Wilson, Org. Biomol. Chem., 2009, 7, 5119–5128.
6. Celia de la Calle Arregui, Jonathan A. Purdie, Catherine A. Haslam, Robert V. Law and John M. Sanderson, Chem. Phys. Lipids, 2016, 195, 58–62

• Biophysics
• Biological Membranes
• Lipids
• Biophysical Chemistry

• 2000: Commitee member of the British Biophysical Society:

Journal Article

• Duché, G., & Sanderson, J. M. (2024). The Chemical Reactivity of Membrane Lipids. Chemical Reviews, 124(6), 2889-3644. https://doi.org/10.1021/acs.chemrev.3c00608
• Sanderson, J. M. (2022). The association of lipids with amyloid fibrils. Journal of Biological Chemistry, 298(8), https://doi.org/10.1016/j.jbc.2022.102108
• Esmaeil, V. S., Britt, H. M., Mosely, J. A., & Sanderson, J. M. (2021). Peptide Lipidation in Lysophospholipid Micelles and Lysophospholipid-Enriched Membranes. Faraday Discussions, 2021(232), 282-294. https://doi.org/10.1039/d1fd00030f
• Rowlands, L. J., Marks, A., Sanderson, J. M., & Law, R. V. (2020). 17O NMR spectroscopy as a tool to study hydrogen bonding of cholesterol in lipid bilayers. Chemical Communications, 56(92), 14499-14502. https://doi.org/10.1039/d0cc05466f
• Britt, H. M., Prakash, A. S., Appleby, S., Mosely, J. A., & Sanderson, J. M. (2020). Lysis of Membrane Lipids Promoted by Small Organic Molecules: Reactivity Depends on Structure but not Lipophilicity. Science Advances, 6(17), Article eaaz8598. https://doi.org/10.1126/sciadv.aaz8598
• Sanderson, J. M. (2020). Far From Inert: Membrane Lipids Possess Intrinsic Reactivity That Has Consequences For Cell Biology. BioEssays, 42(3), Article 1900147. https://doi.org/10.1002/bies.201900147
• Britt, H. M., García-Herrero, C. A., Denny, P. W., Mosely, J. A., & Sanderson, J. M. (2019). Lytic reactions of drugs with lipid membranes. Chemical Science, 10(3), 674-680. https://doi.org/10.1039/c8sc04831b
• Britt, H. M., Mosely, J. A., & Sanderson, J. M. (2019). The Influence of Cholesterol on Melittin Lipidation in Neutral Membranes. Physical Chemistry Chemical Physics, 21(2), 631-640. https://doi.org/10.1039/c8cp06661b
• Ismail, V. S., Mosely, J. A., Tapodi, A., Quinlan, R. A., & Sanderson, J. M. (2016). The Lipidation Profile of Aquaporin-0 Correlates with The Acyl Composition of Phosphoethanolamine Lipids in Lens Membranes. BBA - Biomembranes, 1858(11), 2763-2768. https://doi.org/10.1016/j.bbamem.2016.06.026
• Pridmore, C. J., Rodger, A., & Sanderson, J. M. (2016). The Association of Defensin HNP-2 with Negatively Charged Membranes: A Combined Fluorescence and Linear Dichroism Study. BBA - Biomembranes, 1858(4), 892-903. https://doi.org/10.1016/j.bbamem.2016.01.014
• de la Calle Arregui, C., Purdie, J. A., Haslam, C. A., Law, R. V., & Sanderson, J. M. (2015). Optimised conditions for the synthesis of 17O and 18O labelled cholesterol. Chemistry and Physics of Lipids, 195, 58-62. https://doi.org/10.1016/j.chemphyslip.2015.12.003
• Curtis, F., Malay, A., Trotter, A., Wilson, L., Barradell-Black, M., Bowers, L., …Sharples, G. (2014). Phage Orf family recombinases: conservation of activities and involvement of the central channel in DNA binding. PLoS ONE, 9(8), Article e102454. https://doi.org/10.1371/journal.pone.0102454
• Dods, R., Bechinger, B., Mosely, J., & Sanderson, J. (2013). Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process. Journal of Molecular Biology, 425(22), 4379-4387. https://doi.org/10.1016/j.jmb.2013.07.013
• Sanderson, J. M. (2012). Resolving the kinetics of lipid, protein and peptide diffusion in membranes. Molecular membrane biology, 29(5), 118-143. https://doi.org/10.3109/09687688.2012.678018
• Dods, R., Mosely, J., & Sanderson, J. (2012). The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis. Organic and Biomolecular Chemistry, 10(28), 5371-5378. https://doi.org/10.1039/c2ob07113d
• Carr, R., Di Bari, L., Lo Piano, S., Parker, D., Peacock, R., & Sanderson, J. (2012). A chiral probe for the acute phase proteins alpha-1-acid glycoprotein and alpha-1-antitrypsin based on europium luminescence. Dalton Transactions, 41(42), 13154-13158. https://doi.org/10.1039/c2dt30143a
• Pridmore, C. J., Mosely, J. A., & Sanderson, J. M. (2011). The reproducibility of phospholipid analyses by MALDI-MSMS. Analyst, 136(12), 2598-2605. https://doi.org/10.1039/c0an00436g
• Pridmore, C. J., Mosely, J. A., Rodger, A., & Sanderson, J. M. (2011). Acyl transfer from phosphocholine lipids to melittin. Chemical Communications, 47(5), 1422-1424. https://doi.org/10.1039/c0cc04677a
• McPhee, H., Carlisle, J., Beeby, A., Money, V., Watson, M., Yeo, R., & Sanderson, J. (2011). Influence of Lipids on the Interfacial Disposition of Respiratory Syncytical Virus Matrix Protein. Langmuir, 27(1), 304-311. https://doi.org/10.1021/la104041n
• Damianoglou, A., Rodger, A., Pridmore, C., Dafforn, T. R., Mosely, J. A., Sanderson, J. M., & Hicks, M. R. (2010). The Synergistic Action of Melittin and Phospholipase A2 with Lipid Membranes: Development of Linear Dichroism for Membrane-Insertion Kinetics. Protein and Peptide Letters, 17(11), 1351-1362. https://doi.org/10.2174/0929866511009011351
• Blaser, G., Sanderson, J. M., & Wilson, M. R. (2009). Free-Energy Relationships for the Interactions of Tryptophan with Phosphocholines. Organic and Biomolecular Chemistry, 7(24), 5119-5128. https://doi.org/10.1039/b913919b
• Money, V., McPhee, H., Mosely, J., Sanderson, J., & Yeo, R. (2009). Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction. Proceedings of the National Academy of Sciences, 106(11), 4441-4446. https://doi.org/10.1073/pnas.0805740106
• Ennaceur, S. M., Hicks, M. R., Pridmore, C. J., Dafforn, T. R., Rodger, A., & Sanderson, J. M. (2009). Peptide Adsorption to Lipid Bilayers: Slow Processes Revealed by Linear Dichroism Spectroscopy. Biophysical Journal, 96(4), 1399-1407. https://doi.org/10.1016/j.bpj.2008.10.039
• Blaser, G., Sanderson, J., Batsanov, A., & Howard, J. (2008). The Facile Synthesis of a Series of Tryptophan Derivatives. Tetrahedron Letters, 49(17), 2795-2798. https://doi.org/10.1016/j.tetlet.2008.02.120
• Jackson, T., Sanderson, J., & Kataky, R. (2008). A Gramicidin Analogue that Exhibits Redox Potential Dependent Cation Influx. Sensors and Actuators B: Chemical, 130(2), 630-637. https://doi.org/10.1016/j.snb.2007.10.019
• Sanderson, J. (2007). Refined models for the preferential interactions of tryptophan with phosphocholines. Organic and Biomolecular Chemistry, 5(20), 3276- 3286. https://doi.org/10.1039/b707502b
• Tholozan, F., Sanderson, J., & Quinlan, R. (2007). Focus on Molecules : FoxE3. Experimental Eye Research, 84, 799-800. https://doi.org/10.1016/j.exer.2006.01.022
• Sanderson, J. (2005). Peptide-lipid interactions: insights and perspectives. Organic and Biomolecular Chemistry, 3(2), 201-212. https://doi.org/10.1039/b415499a
• Sanderson, J., Findlay, J., & Fishwick, C. (2005). Preparation of Novel 3H-Trifluoromethyldiazirine-Based Photoactivatable Potassium Channel Antagonists. Tetrahedron, 61(47), 11244-11252. https://doi.org/10.1016/j.tet.2005.09.007
• Cameron, N., Spain, S., Bayley, J., Watson, H., Dureault, A., Sanderson, J., …van Hest, J. (2005). Well Defined Bioactive Polymers by RAFT Polymerization. Abstracts of papers - American Chemical Society, 230, U4302-U4302
• Ennaceur, S., & Sanderson, J. (2005). Micellar aggregates formed following the addition of hexafluoroisopropanol to phospholipid membranes. Langmuir, 21(2), 552-561. https://doi.org/10.1021/la048109y
• Sanderson, J., & Whelan, E. (2004). Characterisation of the Interactions of Aromatic Amino Acids with Diacetyl Phosphatidylcholine. Physical Chemistry Chemical Physics, 6(5), 1012-1017. https://doi.org/10.1039/b312184d
• Hodgson, D., & Sanderson, J. (2004). The Synthesis of Peptides and Proteins Containing Non-Natural Amino Acids. Chemical Society Reviews, 33(7), 422-430. https://doi.org/10.1039/b312953p
• Sanderson, J., & Ward, A. (2004). Analysis of Liposomal Membrane Composition Using Raman Tweezers. Chemical Communications, 1120-1121. https://doi.org/10.1039/b316757g
• Sanderson, J., & Yazdani, S. (2004). The Design, Synthesis and Characterisation of Channel-Forming Peptides. Chemical Communications, 1154-1155. https://doi.org/10.1039/b203046b
• Adams, H., Hunter, C., Lawson, K., Perkins, J., Spey, S., Urch, C., & Sanderson, J. (2001). A Supramolecular System for Quantifying Aromatic Stacking Interactions. Chemistry - A European Journal, 7(22), 4863-4877. https://doi.org/10.1002/1521-3765%2820011119%297%3A22%3C4863%3A%3Aaid-chem4863%3E3.0.co%3B2-3
• Marchi-Artzner, V., T. Gulik-Krzywicki, T., Guedeau-Boudeville, M., Gosse, C., Sanderson, J., Dedieu, J., & Lehn, J. (2001). Selective Adhesion, Lipid Exchange and Membrane-Fusion Processes Between Vesicles of Various Sizes Bearing Complementary Molecular Recognition Groups. ChemPhysChem, 2(6), 367-376. https://doi.org/10.1002/1439-7641%2820010618%292%3A6%3C367%3A%3Aaid-cphc367%3E3.0.co%3B2-%23
• Adams, H., Blanco, J., Chessari, G., Hunter, C., Low, C., Sanderson, J., & Vinter, J. (2001). Quantitative Determination of Intermolecular Interactions with Fluorinated Aromatic Rings. Chemistry - A European Journal, 7(16), 3494-3503. https://doi.org/10.1002/1521-3765%2820010817%297%3A16%3C3494%3A%3Aaid-chem3494%3E3.0.co%3B2-2
• Sanderson, J., Singh, P., Fishwick, C., & Findlay, J. (2000). The synthesis and reactivity of optically pure amino acids bearingside-chain thioamides. Perkin 1, 3227-3231. https://doi.org/10.1039/b004688o
• Fishwick, C., Sanderson, J., & Findlay, J. (1994). An Efficient Route To S-N-(9-Fluorenylmethoxycarbonyl)-4'-(1-Azi-2,2,2-Trifluoroethyl)phenylalanine. Tetrahedron Letters, 35(26), 4611-4614. https://doi.org/10.1016/s0040-4039%2800%2960743-8