Nature Communications (May 2017)
Efficient protein production inspired by how spiders make silk
- Nina Kronqvist,
- Médoune Sarr,
- Anton Lindqvist,
- Kerstin Nordling,
- Martins Otikovs,
- Luca Venturi,
- Barbara Pioselli,
- Pasi Purhonen,
- Michael Landreh,
- Henrik Biverstål,
- Zigmantas Toleikis,
- Lisa Sjöberg,
- Carol V. Robinson,
- Nicola Pelizzi,
- Hans Jörnvall,
- Hans Hebert,
- Kristaps Jaudzems,
- Tore Curstedt,
- Anna Rising,
- Jan Johansson
Affiliations
- Nina Kronqvist
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- Médoune Sarr
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- Anton Lindqvist
- Spiber Technologies AB
- Kerstin Nordling
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- Martins Otikovs
- Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
- Luca Venturi
- R&D Department, Chiesi Farmaceutici, Largo Belloli 11/A
- Barbara Pioselli
- R&D Department, Chiesi Farmaceutici, Largo Belloli 11/A
- Pasi Purhonen
- Department of Biosciences and Nutrition, Karolinska Institutet, and School of Technology and Health, KTH Royal institute of Technology
- Michael Landreh
- Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
- Henrik Biverstål
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- Zigmantas Toleikis
- Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
- Lisa Sjöberg
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- Carol V. Robinson
- Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
- Nicola Pelizzi
- R&D Department, Chiesi Farmaceutici, Largo Belloli 11/A
- Hans Jörnvall
- Department of Medical Biochemistry and Biophysics, Karolinska Institutet
- Hans Hebert
- Department of Biosciences and Nutrition, Karolinska Institutet, and School of Technology and Health, KTH Royal institute of Technology
- Kristaps Jaudzems
- Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
- Tore Curstedt
- Department of Molecular Medicine and Surgery, Karolinska Institutet at Karolinska University Hospital
- Anna Rising
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- Jan Johansson
- Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
- DOI
- https://doi.org/10.1038/ncomms15504
- Journal volume & issue
-
Vol. 8,
no. 1
pp. 1 – 15
Abstract
The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.
