publication . Article . 2017

Cationization increases brain distribution of an amyloid-beta protofibril selective F(ab')2 fragment

Stina Syvänen; Desirée Edén; Dag Sehlin;
Open Access
  • Published: 01 Jan 2017 Journal: Biochemical and Biophysical Research Communications, volume 493, pages 120-125 (issn: 0006-291X, Copyright policy)
  • Publisher: Elsevier BV
  • Country: Norway
Abstract
Antibodies and fragments thereof are, because of high selectivity for their targets, considered as potential therapeutics and biomarkers for several neurological disorders. However, due to their large molecular size, antibodies/fragments do not easily penetrate into the brain. The aim of the present study was to improve the brain distribution via adsorptive-mediated transcytosis of an amyloid-beta (A beta) protofibril selective F(ab')2 fragment (F(ab')2-h158). F(ab')2-h158 was cationized to different extents and the specific and unspecific binding was studied in vitro. Next, cationized F(ab')2-h158 was labelled with iodine-125 and its brain distribution and phar...
Subjects
free text keywords: Cationization, Adsorptive-mediated transcytosis, Alzheimer's disease, Amyloid-beta protofibrils, Molecular imaging, Blood-brain barrier, Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy), Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci), Biophysics, Cell Biology, Biochemistry, Molecular Biology, Chemistry, Amyloid beta, biology.protein, biology
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publication . Article . 2017

Cationization increases brain distribution of an amyloid-beta protofibril selective F(ab')2 fragment

Stina Syvänen; Desirée Edén; Dag Sehlin;