Anna Rising

Anna Rising

Researcher | Docent
Visiting address: Blickagången 16, 14152 Flemingsberg
Postal address: H7 Medicin, Huddinge, H7 BioNut Rising, 171 77 Stockholm

About me

  • Find out more about my research at my group page.

    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


  • Spider silk is well known for its extreme mechanical properties, this natural fiber is tougher than any other man-made fiber. This makes the fiber interesting as a high-performance sustainable fiber for technical applications, but spider silk has also been used in traditional medicine to stop bleedings and to improve wound healing. Silk reeled from spiders has successfully been employed to achieve nerve regeneration in both animal models and patients.

    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 some of 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. At SLU in Uppsala, we develop these fibers for technical applications ( At our lab at Karolinska Institutet, we produce fibers for development of treatments of injuries for which there is no or poor treatment options available due to the lack of suitable materials. Examples include critical sized peripheral nerve and bone defects.

    We are also interested in increasing our understanding of basic silk biology. During the past 400 million years spiders have evolved strategies to cope with massive protein production, storage and precise control of polymerization. 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, but also improve the artificial spider silk fibers we produce today.

    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.

    Recently, we discovered that recombinant spider silk proteins form hydrogels when incubated at 37 degrees Celsius. This makes them very interesting for the development of injectables. Furthermore, the silk proteins can be fused to other proteins of interest and still form hydrogels. The hydrogels are in these cases composed of nano-sized fibrillar networks (composed of the spider silk proteins) which are highly decorated with the fusion protein moiety. We have also shown that stem cells can be successfully encapsulated in the gel with a high survival rate.


All other publications



  • Researcher, Department of Medicine, Huddinge, Karolinska Institutet, 2024-

Degrees and Education

  • Docent, Sveriges Lantbruksuniversitet (SLU), 2013

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