Our research aims to design proteins for medical applications. We currently focus on tailormaking probes for radionucleide molecular imaging(1) and immunotoxins and antibody drug conjugates for cancer therapy(2). Recently, we have also developed a fusion-partner for FcRn-mediated half-life extension of protein drugs that we are currently exploring for a number of different applications (3-4).
Selected recent publications:
Mitran B. et al. Evaluation of 99mTc-Z IGF1R:4551-GGGC affibody molecule, a new probe for imaging of insulin-like growth factor type 1 receptor expression. Amino Acids. 2015 Feb;47(2):303-15.
Hofström C. et al. HAHAHA, HEHEHE, HIHIHI or HKHKHK: influence of position and composition of histidine containing tags on biodistribution of [99mTc(CO)3]+- labeled affibody molecules. J Med Chem. 2013 Jun 27;56(12):4966-74.
Orlova A. et al. [99mTc(CO)3]+-(HE)3-ZIGF1R:4551, a new Affibody conjugate for visualization of insulin-like growth factor-1 receptor expression in malignant tumours. Eur J Nucl Med Mol Imaging. 2013 Feb;40(3):439-49.
Liu H. et al. Potent and specific fusion toxins consisting of a HER2-binding ABD-derived affinity protein (ADAPT), fused to truncated versions of Pseudomonas exotoxin A. In press in International journal of oncology.
Altai M. et al. Affibody-derived drug conjugates: Potent cytotoxic molecules for treatment of HER2 over-expressing tumors. J Control Release. 2018 Oct 28;288:84-95.
Ståhl S. et al. Affibody Molecules in Biotechnological and Medical Applications. Trends Biotechnol. 2017 Aug;35(8):691-712.
Altai M, Liu H, Orlova A, Tolmachev V, Gräslund T. Influence of molecular design on biodistribution and targeting properties of an Affibody-fused HER2-recognising anticancer toxin. Int J Oncol. 2016 Sep;49(3):1185-94.
Liu H. et al. Target-specific cytotoxic effects on HER2-expressing cells by the tripartite fusion toxin ZHER2:2891-ABD-PE38X8, including a targeting affibody molecule and a half-life extension domain. Int J Oncol. 2015 Jun 4. doi: 10.3892/ijo.2015.3027.
Seijsing J et al.. In vivo depletion of serum IgG by an affibody molecule binding the neonatal Fc receptor. Sci Rep. 2018 Mar 23;8(1):5141.
Seijsing et al. An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein. Proc Natl Acad Sci U S A. 2014 Dec 2;111(48):17110-5.
Seijsing J. et al. Robust expression of the human neonatal Fc receptor in a truncated soluble form and as a full-length membrane-bound protein in fusion with eGFP. PLoS One. 2013 Nov 18;8(11):e81350.
(4, In Swedish)
Degree Project in Biotechnology, Second Cycle (BB201X), examiner, course responsible | Course web