Sarah Perrett, PhD
Professor, Institute of Biophysics, CAS

Email: sperrett [at]
Telephone: 010-64889870
Address: Institute of Biophysics, Chinese Academy of Sciences, 
15 Datun Road, Chaoyang District, Beijing 
Postcode: 100101

Research Areas

Protein folding, post-translational modification and quality control
Molecular mechanism of prion propagation
Structure and assembly of functional amyloids


MA, PhD - University of Cambridge


Work Experience

1996-1997, Post-doctoral Research Associate, University of Cambridge

1997-2000, College Research Fellow, University of Cambridge

2000-2003, 1851/Royal Society Research Fellow, Institute of Biophysics, CAS

2003-present, PI, Institute of Biophysics, CAS

2015-present, Professor, University of the Chinese Academy of Science

Teaching Experience

2015-present UCAS Undergraduate Biochemistry (Protein Structure, Function & Folding; Enzymes)

2013-2015       Peking University Undergraduate Biochemistry (Seminar Class: "Classical Papers in Biochemistry")

Honors & Distinctions

2017    Fellow of the Royal Society of Chemistry (FRSC)

2015    Queen's New Years Honours List: OBE for services to UK/China relations in the scientific field

2015    CAS Young International Scientific Collaborator Prize (with Prof. T. Knowles, University of Cambridge)

Selected Publications

1. Yang, J., Dear, A.J., Michaels, T.C.T., Dobson, C.M., Knowles, T.P.J.K.*, Wu, S.* & Perrett, S.* (2018). Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2. J. Am. Chem. Soc. 140, 2493-2503.


2.     Xu, L., Gong, W.*, Cusack, S.A., Wu, H., Loovers, H.M., Zhang, H., Perrett, S., & Jones G.W.* (2018). The β6/β7 region of the Hsp70 substrate-binding domain mediates heat shock response and prion propagation. Cell. Mol. Life Sci. 75, 1445-1459.


3.     Lou, F., Yang, J., Wu, S.* & Perrett, S.* (2017). A co-expression strategy to acheive labeling of individual subunits within a dimeric protein for single molecule analysis. ChemComm 53, 7971-8094.


4. Yang, W., Willemse J., Sawyer E.B., Lou F., Gong, W., Zhang, H., Gras, S.L.*, Claessen, D.* & Perrett, S.* (2017). The propensity of the bacterial rodlin protein RdlB to form amyloid fibrils determines its function in Streptomyces coelicolor. Scientific Reports 7, 42867.


5. Zhang, H., Yang, J., Si, W., Gong, W., Chen, C.* & Perrett, S.* (2016). Glutathionylation of the bacterial Hsp70 chaperone DnaK provides a link between oxidative stress and the heat shock response. J. Biol. Chem. 291, 6967-6981. (Selected for J. Biol. Chem. Protein Folding in the Cell virtual issue.)


6. Wu, H., Gong, W., Wang, J., Perrett, S.* & Feng, Y.* (2016). NMR structure of the C-terminal region of human eukaryotic elongation factor 1Bδ. J. Biomol. NMR 64, 181-187.


7. Rees, J.S., Li, X.W., Perrett, S.,* Lilley, K.S.* & Jackson, A.P.* (2015) Protein neighbours and proximity proteomics. Molecular & Cellular Proteomics 14, 2848-2856. (Invited Review)


8. Zhou, X.M., Shimanovich, U., Herling, T.W., Wu, S., Dobson, C.M., Knowles, T.P.J.* & Perrett, S.* (2015) Enzymatically-active microgels from self-assembling protein nanofibrils for microflow chemistry. ACS Nano, 9, 5772-5781. (Highlighted in Asian Scientist Magazine.)

9. Wu, H., Gong, W., Yao, X., Wang, J., Perrett, S.* & Feng, Y.* (2015). Evolutionarily conserved binding of translationally-controlled tumor protein to eukaryotic elongation factor 1B. J. Biol. Chem. 290, 8694-710.

10. Zhou, X.M., Entwistle, A., Zhang, H., Jackson, A.P., Mason, T.O., Shimanovich, U., Knowles, T.P.J., Smith, A.T., Sawyer, E.B.* & Perrett, S.* (2014). Self-assembly of amyloid fibrils that display active enzymes. ChemCatChem 6, 1961-1968.

11. Li, X.W., Rees, J.S., Lilley, K.S., Howard, J.A., Zhang, H., Peng, X., Hamaia, S.W., Farndale, R.W., Perrett, S.* & Jackson, A.P.* (2014). New insights into the DT40 B cell receptor cluster using a proteomic proximity labeling assay. J. Biol. Chem. 289, 14434-14447. (Highlighted as a Key Scientific Article in Global Medical Discovery. Highlighted in Bulletin of the Chinese Academy of Sciences. Chapter invited for Current Protocols. Review invited for Mol. Cell. Proteom.)

12. Gong, W., Wang, J., Perrett, S.* & Feng, Y.* (2014). Retinoblastoma-binding protein 1 has an interdigitated double Tudor domain with DNA binding activity. J. Biol. Chem. 289, 4882-4895.

13. Xu, L.Q., Wu, S., Buell, A.K., Cohen, S.I.A., Chen, L.J., Hu, W.H., Cusack, S.A., Itzhaki, L.S., Zhang, H.*, Knowles, T.P.J., Dobson, C.M., Welland, M.E., Jones, G.W. & Perrett S.* (2013). Influence of specific Hsp70 domains on fibril formation of the yeast prion protein Ure2. Phil. Trans. Roy. Soc. B 368, 20110410. (Invited submission)

14. Zhou, Q., Hu, M., Zhang, W., Jiang, L., Perrett, S., Zhou, J., Wang, J.* (2013) Probing the function of a tyrosine-cysteine crosslink in metalloenzymes through the genetic incorporation of 3-methylthiotyrosine. Angew. Chem. Int. Ed. Engl. 52, 1203-1207.

15. Zhu, M., Perrett, S. & Nie, G.* (2013). Understanding the particokinetics of engineered nanomaterials for safe and effective therapeutic applications. SMALL 9, 1619-34.

16. Truman, A.W., Kristjansdottir, K., Wolfgeher, D., Hasin, N., Polier, S., Zhang, H., Perrett, S., Prodromou, C., Jones, G.W. & Kron, S.J.* (2012). CDK-dependent Hsp70 phosphorylation controls G1 cyclin abundance and cell cycle progression. CELL 151, 1308-1318. (Recommended as a New Finding by F1000.)

17. Sawyer, E.B., Claessen D., Gras, S.L. & Perrett, S.* (2012) Exploiting amyloid: How and why bacteria use cross-β fibrils. Biochem. Soc. Trans. 40, 728-34. (Invited Review)

18. Gong, W., Zhou, T., Mo, J., Perrett, S., Wang, J.* & Feng, Y.* (2012). Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1. J. Biol. Chem. 287, 8531-8540.

19. Chen, L.J., Sawyer, E.B. and Perrett, S.* (2011). The yeast prion protein Ure2: insights into the mechanism of amyloid formation. Biochem. Soc. Trans. 39, 1359-1364. (Invited review)

20. Li, Y., Zhou, Y., Wang, H.Y., Perrett, S., Zhao, Y.,* Tang, Z.,* and Nie, G.* (2011). Chirality of gluthathione surface coating affects the cytotoxicity of quantum dots. Angew. Chem. Int. Ed. Engl. 50, 5860-5864. (Highlighted in Nature Materials (2011) 10, 480.)

21. Wang, Y.Q., Buell, A.K., Wang, X.Y., Welland M.E., Dobson, C.M., Knowles, T.P.J.* and Perrett, S.* (2011). Relationship between prion propensity and the rates of individual molecular steps of fibril assembly. J. Biol. Chem. 286, 12101-12107. (On the Cover.)

22. Zhang, H., Xu, L.Q. and Perrett, S.* (2011). Studying the effects of chaperones on amyloid fibril formation. Methods 53, 285-294. (Invited Review)

23. Zhang, Z.R. and Perrett, S.* (2009). Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils. J. Biol. Chem. 284, 14058-14067.

24. Fei, L. and Perrett, S.* (2009). Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils due to proximity of a potential amyloid stretch. J. Biol. Chem. 284, 11134-11141.

25. Fei, L. and Perrett, S.* (2009). Effect of nanoparticles on protein folding and fibrillogenesis. Int. J. Mol. Sci. 10, 646-655. (Invited Review)

26. Perrett, S.* & Jones, G.W.* (2008). Insights into the mechanism of prion propagation. Curr. Opin. Struct. Biol. 18, 52-59. (Invited Review)

27. Gao, L., Zhuang, J., Nie, L., Zhang, J., Gu, N., Wang, T., Perrett, S.* & Yan, X.* (2007). Intrinsic peroxidase-like activity of ferromagnetic nanoparticles. Nature Nanotechnology 2, 577-583. (Article)