Gefei Chen

Gefei Chen

Assistant professor

Research description

Research group

Surveillance by molecular chaperones may decline, and proteins misfold and self-assemble into amorphous aggregates as well as fibrillar amyloid which are linked to cureless human diseases. Our research aims to understand how molecular chaperones interfere with different types of protein aggregation and alleviate relevant toxicities, and augment specific chaperone capacity for novel treatment developments, in particular against cancer and neurodegenerative diseases. On the other side, non-pathological amyloid is supposed to be shared by spider silk, one of the toughest biomaterials. Currently, our understanding of amyloid-like formation during spider silk assembly process and underlying mechanisms are largely missing.


[1]    Cai H#, Chen G#, Yu H, Tang Y, Xiong S, Qi X. One-step heating strategy for efficient solubilization of recombinant spider silk protein from inclusion bodies[J]. BMC Biotechnology, 2020, 20(1):37. (#equal contributions)

[2]    Andrade-Talavera Y, Arroyo-García L, Chen G, Johansson J, Fisahn A. Modulation of Kv3.1/Kv3.2 promotes gamma oscillations by rescuing Aβ-induced desynchronization of fast-spiking interneuron firing in an AD mouse model[J]. The Journal of Physiology, 2020, 598(17):3711-3725.

[3]    Poska H, Leppert A, Tigro H, Zhong X, Kaldmäe M, Nilsson H, Hebert H, Chen G, Johansson J. Recombinant Bri3 BRICHOS domain is a bifunctional molecular chaperone[J]. Scientific Reports, 2020, 10(1): 9817.

[4]    Chen G, Andrade-Talavera Y, Tambaro S, Leppert A, Nilsson H, Zhong X, Landreh M, Nilsson P, Hebert H, Biverstål H, Fisahn A, Abelein A, Johansson J. Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro[J]. Communications Biology, 2020, 3(1): 32.

[5]    Abelein A, Chen G, Kitoka K, Aleksis R, Oleskovs F, Sarr M, Landreh M, Pahnke J, Nordling K, Kronqvist N, Jaudzems K, Rising A, Johansson J, Biverstål H. High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain[J]. Scientific Reports, 2020, 10(1):235.

[6]    Kaldmäe M, Leppert A, Chen G, Sarr M, Sahin C, Nordling K, Kronqvist N, Gonzalvo-Ulla M, Fritz N, Abelein A, Laίn S, Biverstål H, Jörnvall H, Lane DP, Rising A, Johansson J, Landreh M. High intracellular stability of the spidroin N-terminal domain in spite of abundant amyloidogenic segments revealed by in-cell hydrogen/deuterium exchange mass spectrometry[J]. The FEBS Journal, 2020, 287(13):2823-2833.

[7]    Leppert A, Chen G, Johansson J. BRICHOS: a chaperone with different activities depending on quaternary structure and cellular location?[J]. Amyloid, 2019, 26(sup1):152-153.

[8]    Tambaro S, Galan-Acosta L, Leppert A, Chen G, Biverstål H, Presto J, Nilsson P, Johansson J. Blood-brain and blood-cerebrospinal fluid passage of different BRICHOS molecular chaperone domains[J]. The Journal of Biological Chemistry, 2019, 294(8): 2606-2615.

[9]    Balleza-Tapia H, Crux S, Andrade-Talavera Y, Dolz-Gaiton P, Papadia D, Chen G, Johansson J, Fisahn A. TrpV1 receptor activation rescues neuronal function and network gamma oscillations from Aβ-induced impairment in mouse hippocampus in vitro[J]. eLife, 2018, 7: e37703.

[10]    Sarr M, Kronqvist N, Chen G, Aleksis R, Purhonen P, Hebert H, Jaudzems K, Rising A, Johansson J. A spidroin-derived solubility tag enables controlled aggregation of a designed amyloid protein[J]. The FEBS Journal, 2018, 285(10): 1873-1885.

[11]    Chen G, Abelein A, Nilsson H, Leppert A, Andrade-Talavera Y, Tambaro S, Hemmingsson L, Roshan F, Landreh M, Biverstål H, Koeck P, Presto J, Hebert H, Fisahn A, Johansson J. Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state[J]. Nature Communications, 2017, 8: 2081.

[12]    Poska H, Haslbeck M, Kurudenkandy FR, Hermansson E, Chen G, Kostallas G, Abelein A, Biverstål H, Crux S, Fisahn A, Presto J, Johansson J. Dementia related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Abeta42 toxicity in Drosophila[J]. Biochemical Journal, 2016, 473(20): 3683-3704.

[13]    Lin S, Chen G, Liu X, Meng Q. Chimeric spider silk proteins mediated by intein result in artificial hybrid silks[J]. Biopolymers, 2016, 105(7): 385-392.

[14]    Otikovs M#, Chen G#, Nordling K, Landreh M, Meng Q, Jörnvall H, Kronqvist N, Rising A, Johansson J, Jaudzems K. Back Cover: Diversified structural basis of a conserved molecular mechanism for ph-dependent dimerization in spider silk N-terminal domains[J]. ChemBioChem, 2015, 16(12): 1720-1724. (#equal contributions)

[15]    Andersson M#, Chen G#, Otikovs M, Landreh M, Nordling K, Kronqvist N, Westermark P, Jörnvall H, Knight S, Ridderstråle Y, Holm L, Meng Q, Jaudzems K, Chesler M, Johansson J, Rising A. Carbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domains[J]. PLoS Biology, 2014, 12(8): e100192.(#equal contributions)

[16]    Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K, Landreh M, Sarr M, Jörnvall H, Wennmalm S, Widengren J, Meng Q, Rising A, Otzen D, Knight SD, Jaudzems K, Johansson J. Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation[J]. Nature communications, 2014, 5: 3254.

[17]    Chen G, Liu X, Zhang Y, Lin S, Yang Z, Johansson J, Rising A, Meng Q. Full-length minor ampullate spidroin gene sequence[J]. PLoS ONE, 2012, 7(12): e52293.



Our projects are financially supported by Olle Engkvists Stiftelse, Petrus och Augusta Hedlunds Stiftelse, Alzheimerfonden, Åhlén-stiftelsens, Loo and Hans Osterman Foundation for Medical Research, Gun and Bertil Stohne's Foundation, Magnus Bergvalls Stiftelse, Karolinska Institutet Research Foundation Grants, Foundation for Geriatric Diseases at Karolinska Institutet, and Stiftelsen för Gamla Tjänarinnor.