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Research description

Spider silk is well known for its extreme mechanical properties, this natural fiber is tougher than any other man-made fiber. Spider silk has also been used in traditional medicine to stop bleedings and to imprive wound healing. In animal studies, silk reeled from spiders has succesfully been employed to achieve nerve regeneration of injured peripheral nerves. I study spider silk with the aim to generate a biomaterial to be used in regenerative medicine and as matrix for cell culture.

We can produce artificial spider silk by letting bacteria produce partial spider silk proteins. These proteins self-assemble into fibers that match mammalian tendons in terms of tensile strength. However, to produce more defined fibers that can be employed for medical applications, we need to learn how to control the solubility and assembly of the silk proteins. Spider silk is stored at extreme concentrations (30-50% w/w, in an aqueous solution) in the spider’s silk glands, and is transformed into a solid fiber within fractions of a second in a defined part of the spinning apparatus. Clearly, this process must be highly regulated and we have recently revealed the physiological conditions along the spider silk spinning apparatus, as well as the molecular mechanisms that controls silk fiber formation. Based on these insights we have engineered a biomimetic artificial spinning device in which we can spin hundreds of meters of artificial spider silk. The silk we produce will be tested for the treatment of diseases and injuries for which there is no or poor treatment options available due to the lack of suitable materials. Specifically, we use human pluripotent stem cells and progenitor cells in cell culture experiments were we aim at developing novel treatments for e.g. cardiac disease and spinal cord injuries. By understanding how spiders manage to regulate protein solubility and assembly, we hope to also get insights into how other proteins form aggregates that are associated with disease (e.g. Alzheimer’s disease).

Another line of research concerns the spider silk proteins’ N-terminal domain  (NT). NT plays an important role in fiber formation; it mediates solubility to silk proteins at high pH and rapid fiber formation when the pH is lowered (as in the silk production apparatus). We study NT to understand the molecular mechanisms behind these traits and aim to make use of our findings for biotechnological applications. For example, in one project we employ NT to produce protein-based drugs and drug candidates since NT seems to be Nature´s way of increasing solubility of aggregation prone proteins. Many of the new drugs and drug candidates generated by the pharmaceutical industry are proteins or peptides that quite often are difficult to produce, but by using NT we hope to provide a more efficient and cheap way of production.

Our recent understanding of NT has enabled us to produce artificial lung surfactant in an efficient process at very low cost. This advancement has opened up the possibility to use lung surfactant as a drug delivery vehicle. Lung surfactant spreads very rapidly across a mucosal or serosal surface and it efficiently carries for example some antibiotics and corticosteroids with it. Since lung surfactant for the first time can be produced very cost-efficiently, we are now exploiting this invention to develop a novel drug carrier for the treatment of respiratory disease and we are also investigating if the surfactant preparations we make can be used to treat acute respiratory distress syndrome in adults.


Academic honours, awards and prizes

Selected member of the Young Academy of Sweden 2015-2020.

Medal of Merit in Silver from the Swedish University of Agricultural Sciences, 2012.

Nicholson Award from Rockefeller University in 2012. Award: 25 000 USD.

Best Paper Award 2013. Materials.

Entered the list of Swedens 33 most interesting technology-driven companies in 2012 with  Spiber Technologies AB

Winner of VINN NU competition (VINNOVA) in 2008 with Spiber Technologies AB




Biomimetic spinning of artificial spider silk from a chimeric minispidroin
Andersson M, Jia Q, Abella A, Lee Xy, Landreh M, Purhonen P, et al
Nature chemical biology 2017;13(3):262-264

Mass spectrometry captures structural intermediates in protein fiber self-assembly
Landreh M, Andersson M, Marklund Eg, Jia Q, Meng Q, Johansson J, et al
Chemical communications (Cambridge, England) 2017;53(23):3319-3322

Novel expression of a functional trimeric fragment of human SP-A with efficacy in neutralisation of RSV
Watson A, Kronqvist N, Spalluto Cm, Griffiths M, Staples Kj, Wilkinson T, et al
Immunobiology 2017;222(2):111-118

Efficient passage of human pluripotent stem cells on spider silk matrices under xeno-free conditions
Wu S, Johansson J, Hovatta O, Rising A
Cellular and molecular life sciences : CMLS 2016;73(7):1479-88

Silk Spinning in Silkworms and Spiders
Andersson M, Johansson J, Rising A
International journal of molecular sciences 2016;17(8):-

Transmissible amyloid
Tjernberg Lo, Rising A, Johansson J, Jaudzems K, Westermark P
Journal of internal medicine 2016;280(2):153-63

Carbonic anhydrase generates a pH gradient in Bombyx mori silk glands
Domigan Lj, Andersson M, Alberti Ka, Chesler M, Xu Q, Johansson J, et al
Insect biochemistry and molecular biology 2015;65():100-6

Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains
Otikovs M, Chen G, Nordling K, Landreh M, Meng Q, Jörnvall H, et al
Chembiochem : a European journal of chemical biology 2015;16(12):1720-4

Specific chaperones and regulatory domains in control of amyloid formation
Landreh M, Rising A, Presto J, Jörnvall H, Johansson J
The Journal of biological chemistry 2015;290(44):26430-6

Toward spinning artificial spider silk
Rising A, Johansson J
Nature chemical biology 2015;11(5):309-15

Carbonic anhydrase generates CO2 and H+ that drive spider silk formation via opposite effects on the terminal domains
Andersson M, Chen G, Otikovs M, Landreh M, Nordling K, Kronqvist N, et al
PLoS biology 2014;12(8):e1001921-

Controlled assembly: a prerequisite for the use of recombinant spider silk in regenerative medicine?
Rising A
Acta biomaterialia 2014;10(4):1627-31

Evaluation of Functionalized Spider Silk Matrices: Choice of Cell Types and Controls are Important for Detecting Specific Effects
Johansson J, Rising A
Frontiers in bioengineering and biotechnology 2014;2():50-

Recombinant spider silk genetically functionalized with affinity domains
Jansson R, Thatikonda N, Lindberg D, Rising A, Johansson J, Nygren PÅ, et al
Biomacromolecules 2014;15(5):1696-706

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation
Kronqvist N, Otikovs M, Chmyrov V, Chen G, Andersson M, Nordling K, et al
Nature communications 2014;5():3254-

Spider silk for xeno-free long-term self-renewal and differentiation of human pluripotent stem cells
Wu S, Johansson J, Damdimopoulou P, Shahsavani M, Falk A, Hovatta O, et al
Biomaterials 2014;35(30):8496-502

Morphology and Composition of the Spider Major Ampullate Gland and Dragline Silk
Andersson M, Holm L, Ridderstrale Y, Johansson J, Rising A
BIOMACROMOLECULES 2013;14(8):2945-52

Control of amyloid assembly by autoregulation
Landreh M, Johansson J, Rising A, Presto J, Jörnvall H
The Biochemical journal 2012;447(2):185-92

Full-Length Minor Ampullate Spidroin Gene Sequence
Chen Gf, Liu Xq, Zhang Yl, Lin Sz, Yang Zj, Johansson J, et al
PLOS ONE 2012;7(12):e52293-

Invited Review Current Progress and Limitations of Spider Silk for Biomedical Applications
Widhe M, Johansson J, Hedhammar M, Rising A
BIOPOLYMERS 2012;97(6):468-78

pH-Dependent Dimerization of Spider Silk N-Terminal Domain Requires Relocation of a Wedged Tryptophan Side Chain
Jaudzems K, Askarieh G, Landreh M, Nordling K, Hedhammar M, Jornvall H, et al

Recombinant spider silk matrices for neural stem cell cultures
Lewicka M, Hermanson O, Rising Au
Biomaterials 2012;33(31):7712-7

Functionalisation of recombinant spider silk with conjugated polyelectrolytes
Muller C, Jansson R, Elfwing A, Askarieh G, Karlsson R, Hamedi M, et al

Spider silk proteins: recent advances in recombinant production, structure-function relationships and biomedical applications
Rising A, Widhe M, Johansson J, Hedhammar M

A pH-Dependent Dimer Lock in Spider Silk Protein
Landreh M, Askarieh G, Nordling K, Hedhammar M, Rising A, Casals C, et al

Recombinant spider silk as matrices for cell culture
Widhe M, Bysell H, Nystedt S, Schenning I, Malmsten M, Johansson J, et al
BIOMATERIALS 2010;31(36):9575-85

Self-assembly of spider silk proteins is controlled by a pH-sensitive relay
Askarieh G, Hedhammar M, Nordling K, Saenz A, Casals C, Rising A, et al
NATURE 2010;465(7295):236-8

Tissue Response to Subcutaneously Implanted Recombinant Spider Silk: An in Vivo Study
Fredriksson C, Hedhammar M, Feinstein R, Nordling K, Kratz G, Johansson J, et al
MATERIALS 2009;2(4):1908-1922

Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis: Implications for fiber formation
Hedhammar M, Rising A, Grip S, Martinez As, Nordling K, Casals C, et al
BIOCHEMISTRY 2008;47(11):3407-17

Macroscopic fibers self-assembled from recombinant miniature spider silk proteins
Stark M, Grip S, Rising A, Hedhammar M, Engstrom W, Hjalm G, et al
BIOMACROMOLECULES 2007;8(5):1695-701

Major ampullate spidroins from Euprosthenops australis: multiplicity at protein, mRNA and gene levels
Rising A, Johansson J, Larson G, Bongcam-rudloff E, Engstroem W, Hjalmt G

N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins
Rising A, Hjalm G, Engstrom W, Johansson J
BIOMACROMOLECULES 2006;7(11):3120-4

Spider silk proteins - Mechanical property and gene sequence
Rising A, Nimmervoll H, Grip S, Fernandez-arias A, Storckenfeldt E, Knight Dp, et al
ZOOLOGICAL SCIENCE 2005;22(3):273-81

The JNK interacting protein JIP-1 and insulin like growth factor II genes are co-expressed in human embryonic tumours
Engstrom W, Rising A, Grip S
ANTICANCER RESEARCH 2005;25(2A):1075-8

Expression of JNK interacting protein JIP-1 is Down-regulated in liver from mouse embryos with a disrupted insulin-like growth factor II gene
Rohbe L, Larsson M, Rising A, Grip S, Burns J, Engstrom W
IN VIVO 2004;18(5):643-7

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