Recombinant Spider Silk as Mediator for One‐Step, Chemical‐Free Surface Biofunctionalization

Horak, J., Jansson, R., Dev, A., Nilebäck, L., Behnam, K., Linnros, J., Hedhammar, M., Karlström, A. E.
(2018) Advanced Functional Materials, 1800206,
https://onlinelibrary.wiley.com/doi/abs/10.1002/adfm.201800206

Recombinant spider silk functionalized with a motif from fibronectin mediates cell adhesion and growth on polymeric substrates by entrapping cells during self-assembly

Tasiopoulos, C. P., Widhe, M., Hedhammar, M.
(2018) ACS Applied Materials & Interfaces
https://pubs.acs.org/doi/10.1021/acsami.8b02647, article ASAP

Silk-silk interactions between silkworm fibroin and recombinant spider silk fusion proteins enable construction of bioactive materials

Nilebäck, L., Chouhan, D., Jansson, R., Widhe, M., Mandal, B., Hedhammar, M.
(2017) ACS Applied Materials & Interfaces9 (37), pp 31634–31644
http://pubs.acs.org/doi/abs/10.1021/acsami.7b10874

Efficient protein production inspired by how spiders make silk

Kronqvist, N., Sarr, M., Lindqvist, A., Nordling, K., Otikovs, M., Venturi, L., Pioselli, B., Purhonen, P., Landreh, M., Biverstål, H., Toleikis, Z., Sjöberg, L., Robinson, C.V., Pelizzi, N., Jörnvall, H., Hebert, H., Jaudzems, K., Curstedt, T., Rising, A., Johansson, J.
(2017) Nature communications 8:15504
https://www.nature.com/articles/ncomms15504

Ultrastrong and Bioactive Nanostructured Bio-Based Composites

Mittal, N., Jansson, R., Widhe, M., Benselfelt, T., Håkansson, K.M.O., Lundell, F., Hedhammar, M., Söderberg, L.D.
(2017) ACS Nano, 11 (5), pp 5148–5159
http://pubs.acs.org/doi/abs/10.1021/acsnano.7b02305

Self-assembly of recombinant silk as a strategy for chemical-free formation of bioactive coatings: a real-time study

Nilebäck, L., Hedin, J., Widhe, M., Floderus, L., Krona, A., Bysell, H., Hedhammar, M.
(2017) BioMacromolecules, 18(3), pp. 846-854
https://doi.org/10.1021/acs.biomac.6b01721

Genetic fusion of single-chain variable fragments to partial spider silk improves target detection in micro- and nanoarrays

Thatikonda, N., Delfani, P., Jansson, R., Petersson, L., Lindberg, D., Wingren, C., Hedhammar, M.
(2016) Biotechnology Journal, 11 (3), pp. 437-448
https://doi.org/10.1002/biot.201500297

Efficient passage of human pluripotent stem cells on spider silk matrices under xeno-free conditions

Wu, S., Johansson, J., Hovatta, O., Rising, A.
(2016) Cellular and Molecular Life Sciences, 73 (7), pp. 1479-1488
https://doi.org/10.1007/s00018-015-2053-5

Functionalized silk assembled from a recombinant spider silk fusion protein (Z-4RepCT) produced in the methylotrophic yeast Pichia pastoris

Jansson, R., Lau, C.H., Ishida, T., Ramström, M., Sandgren, M., Hedhammar, M.
(2016) Biotechnology Journal, 11 (5), pp. 687-699
https://doi.org/10.1002/biot.201500412

Rational Design of Spider Silk Materials Genetically Fused with an Enzyme

Jansson, R., Courtin, C.M., Sandgren, M., Hedhammar, M.
(2015) Advanced Functional Materials, 25  (33), pp. 5343-5352
https://doi.org/10.1002/adfm.201501833

Pancreatic islet survival and engraftment is promoted by culture on functionalized spider silk matrices

Johansson, U., Ria, M., Åvall, K., Shalaly, N.D., Zaitsev, S.V., Berggren, P.-O., Hedhammar, M.
(2015) PLoS ONE, 10 (6)
https://doi.org/10.1371/journal.pone.0130169

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., Rising, A.
(2014)Biomaterials, 35 (30), pp. 8496-8502
https://doi.org/10.1016/j.biomaterials.2014.06.039

Recombinant spider silk genetically functionalized with affinity domains

Jansson, R., Thatikonda, N., Lindberg, D., Rising, A., Johansson, J., Nygren, P.-A., Hedhammar, M.
(2014) Biomacromolecules, 15 (5), pp. 1696-1706
https://doi.org/10.1021/bm500114e

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., Jörnvall, H., Rising, A., Knight, S.D., Johansson, J.
(2012) Journal of Molecular Biology, 422 (4), pp. 477-487
https://doi.org/10.1016/j.jmb.2012.06.004

Current progress and limitations of spider silk for biomedical applications

Widhe, M., Johansson, J., Hedhammar, M., Rising, A
(2012) Biopolymers, 97 (6), pp. 468-478
https://doi.org/10.1002/bip.21715

Functionalisation of recombinant spider silk with conjugated polyelectrolytes

Müller, C., Jansson, R., Elfwing, A., Askarieh, G., Karlsson, R., Hamedi, M., Rising, A., Johansson, J., Inganäs, O., Hedhammar, M.
(2011) Journal of Materials Chemistry, 21 (9), pp. 2909-2915
https://doi.org/10.1039/c0jm03270k

Spider silk proteins: Recent advances in recombinant production, structure-function relationships and biomedical applications

Rising, A., Widhe, M., Johansson, J., Hedhammar, M.
(2011) Cellular and Molecular Life Sciences, 68 (2), pp. 169-184
https://doi.org/10.1007/s00018-010-0462-z

A pH-Dependent Dimer Lock in Spider Silk Protein

Landreh, M., Askarieh, G., Nordling, K., Hedhammar, M., Rising, A., Casals, C., Astorga-Wells, J., Alvelius, G., Knight, S.D., Johansson, J., Jörnvall, H., Bergman, T.
(2010) Journal of Molecular Biology, 404 (2), pp. 328-336
https://doi.org/10.1016/j.jmb.2010.09.054

Sterilized recombinant spider silk fibers of low pyrogenicity

Hedhammar, M.Y., Bramfeldt, H., Baris, T., Widhe, M., Askarieh, G., Nordling, K., Aulock, S.V., Johansson, J.
(2010) Biomacromolecules, 11 (4), pp. 953-959
https://doi.org/10.1021/bm9014039

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., Johansson, J., Knight, S.D.
(2010) Nature, 465 (7295), pp. 236-238
https://doi.org/10.1038/nature08962

Recombinant spider silk as matrices for cell culture

Widhe, M., Bysell, H., Nystedt, S., Schenning, I., Malmsten, M., Johansson, J., Rising, A., Hedhammar, M.
(2010) Biomaterials, 31 (36), pp. 9575-9585
https://doi.org/10.1016/j.biomaterials.2010.08.061

Engineered disulfides improve mechanical properties of recombinant spider silk

Grip, S., Johansson, J., Hedhammar, M.
(2009) Protein science, 18 (5), pp. 1012-1022
https://doi.org/10.1002/pro.111

Tissue response to subcutaneously implanted recombinant spider silk: An in vivo study

Fredriksson, C., Hedhammar, M., Feinstein, R., Nordling, K., Kratz, G., Johansson, J., Huss, F., Rising, A.
(2009) Materials, 2 (4), pp. 1908-1922
https://doi.org/10.3390/ma2041908

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, A.S., Nordling, K., Casals, C., Stark, M., Johansson, J.
(2008) Biochemistry, 47 (11), pp. 3407-3417
https://doi.org/10.1021/bi702432y

Major ampullate spidroins from Euprosthenops australis: Multiplicity at protein, mRNA and gene levels

Rising, A., Johansson, J., Larson, G., Bongcam-Rudloff, E., Engström, W., Hjälm, G.
(2007) Insect Molecular Biology, 16 (5), pp. 551-561
https://doi.org/10.1111/j.1365-2583.2007.00749.x

Macroscopic fibers self-assembled from recombinant miniature spider silk proteins

Stark, M., Grip, S., Rising, A., Hedhammar, M., Engström, W., Hjälm, G., Johansson, J.
(2007) Biomacromolecules, 8 (5), pp. 1695-1701
https://doi.org/10.1021/bm070049y

N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins

Rising, A., Hjälm, G., Engström, W., Johansson, J.
(2006) Biomacromolecules, 7 (11), pp. 3120-3124
https://doi.org/10.1021/bm060693x