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  • 1.
    Ekblad, Torun
    et al.
    KTH, School of Biotechnology (BIO).
    Tolmachev, Vladimir
    Uppsala Univ, Rudbeck Lab, Unit Biomed Radiat Sci.
    Orlova, Anna
    Uppsala Univ, Rudbeck Lab, Unit Biomed Radiat Sci.
    Lendel, Christofer
    Univ Cambridge, Dept Chem.
    Abrahmsén, Lars
    Affibody AB.
    Eriksson Karlström, Amelie
    KTH, School of Biotechnology (BIO), Molecular Biotechnology.
    Synthesis and chemoselective intramolecular crosslinking of a HER2-binding Affibody2009In: Biopolymers, ISSN 0006-3525, E-ISSN 1097-0282, Vol. 92, no 2, p. 116-123Article in journal (Refereed)
    Abstract [en]

    The human epidermal growth factor receptor HER2 has emerged as an important target for molecular imaging of breast cancer. This article presents the design and synthesis of a HER2-targeting affibody molecule with improved stability and tumor targeting capacity and with potential use as an imaging agent. The 58 aa three-helix bundle protein was assembled using solid-phase peptide synthesis, and a chemoselective ligation strategy was used to establish an intramolecular thioether bond between the side chain thiol group of a cysteine residue, positioned in the loop between helices I and II, and a chloroacetyl group on the side chain amino group of the C-terminal lysine residue. The tethered protein offered an increased thermal stability, with a melting temperature of 64 degrees C, compared to 54 degrees C for the linear control. The ligation did not have a major influence on the HER2 binding affinity, which was 320 and 380 pM for the crosslinked and linear molecules, respectively. Biodistribution studies were performed both in normal and tumor-bearing mice to evaluate the impact of the crosslinking on the in vivo behavior and on the tumor targeting performance. The distribution pattern was characterized by a low uptake in all organs except kidney, and rapid clearance from blood and normal tissue. Crosslinking of the protein resulted in a significantly increased tumor accumulation, rendering the tethered HER2-binding affibody molecule a valuable lead in the development of superior HER2 imaging agents.

  • 2. Karlsson, J.
    et al.
    Momcilovic, Dane
    Wittgren, B.
    Schulein, M.
    Tjerneld, F.
    Brinkmalm, G.
    Enzymatic degradation of carboxymethyl cellulose hydrolyzed by the endoglucanases Cel5A, Cel7B, and Cel45A from Humicola insolens and Cel7B, Cel12A and Cel45Acore from Trichoderma reesei2002In: Biopolymers, ISSN 0006-3525, E-ISSN 1097-0282, Vol. 63, no 1, p. 32-40Article in journal (Refereed)
    Abstract [en]

    Enzymatic hydrolysis of carboxymethyl cellulose (CMC) has been studied with purified endoglucanases Hi Cel5A (EG II), Hi Cel7B (EG I), and Hi Cel45A (EG V)from Humicola insolens, and Tr Cel7B (EG I), Tr Cel12A (EG III), and Tr Cel45Acore (EG V)from Trichoderma reesei. The CMC, with a degree of substitution (DS) of 0.7, was hydrolyzed with a single enzyme until no further hydrolysis was observed. The hydrolysates were analyzed for production of substituted and non substituted oligosaccharides with size exclusion chromatographly (SEC) and with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF-MS). Production of reducing ends and of nonsubstituted oligosaccharides was determined as well. The two most effective endoglucanases for CMC hydrolysis were Hi Cel5.A and Tr Cel7B. These enzymes degraded CMC to lower molar mass fragments compared with the other endoglucanases. The products had the highest DS determined by MALDI-TOF-MS. Thus, Hi Cel5A and Tr Cel7B were less inhibited by the substituents than the other endoglucanases. The endoglucanase with clearly the lowest activity on CMC was Tr Cel45Acore. It produced less than half of the amount of reducing ends compared to Tr Cel7B; furthermore, the products had significantly lower DS. By MALDI-TOF-MS, oligosaccharide with different degree of polymerization (DP) and with different number of substituents could be separated and identified. The average oligosaccharide DS as function of DP could be measured for each enzyme after hydrolysis. The combination of techniques for analysis of product formation gave information on average length of unsubstituted blocks of CMC.

  • 3.
    Lindgren, Joel
    et al.
    KTH, School of Biotechnology (BIO), Protein Technology.
    Refai, Essam
    Zaitsev, Sergei
    Abrahmsén, Lars
    Berggren, Per-Olof
    Eriksson Karlström, Amelie
    KTH, School of Biotechnology (BIO), Protein Technology.
    A GLP-1 receptor agonist conjugated to an albumin-binding domain for extended half-life2014In: Biopolymers, ISSN 0006-3525, E-ISSN 1097-0282, Vol. 102, no 3, p. 252-259Article in journal (Refereed)
    Abstract [en]

    Glucagon-like peptide 1 (GLP-1) and related peptide agonists have been extensively investigated for glycaemic control in Type 2 diabetes, and may also have therapeutic applications for other diseases. Due to the short half-life (t1/2<2 min) of the endogenous peptide, caused by proteolytic degradation and renal clearance, different strategies for half-life extension and sustained release have been explored. In the present study, conjugates between a GLP-1 analogue and a 5 kDa albumin-binding domain (ABD) derived from streptococcal protein G have been chemically synthesized and evaluated. ABD binds with high affinity to human serum albumin, which is highly abundant in plasma and functions as a drug carrier in the circulation. Three different GLP-1-ABD conjugates, with the two peptides connected by linkers of two, four, and six PEG units, respectively, were synthesized and tested in mouse pancreatic islets at high (11 mM) and low (3 mM) glucose concentration. Insulin release upon stimulation was shown to be glucose-dependent, showing no significant difference between the three different GLP-1-ABD conjugates and unconjugated GLP-1 analogue. The biological activity, in combination with the high affinity binding to albumin, make the GLP-1-ABD conjugates promising GLP-1 receptor agonists expected to show extended in vivo half-life.

  • 4.
    Ravishankar, Harsha
    et al.
    KTH, School of Engineering Sciences (SCI), Applied Physics, Biophysics.
    Barth, Andreas
    Andersson, Magnus
    KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Probing the activity of a recombinant Zn2+-transporting P-type ATPase2017In: Biopolymers, ISSN 0006-3525, E-ISSN 1097-0282Article in journal (Refereed)
1 - 4 of 4
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