| Literature DB >> 24411731 |
Jens Niewoehner1, Bernd Bohrmann2, Ludovic Collin2, Eduard Urich2, Hadassah Sade1, Peter Maier1, Petra Rueger1, Jan Olaf Stracke1, Wilma Lau1, Alain C Tissot1, Hansruedi Loetscher2, Anirvan Ghosh3, Per-Ola Freskgård4.
Abstract
Although biotherapeutics have vast potential for treating brain disorders, their use has been limited due to low exposure across the blood-brain barrier (BBB). We report that by manipulating the binding mode of an antibody fragment to the transferrin receptor (TfR), we have developed a Brain Shuttle module, which can be engineered into a standard therapeutic antibody for successful BBB transcytosis. Brain Shuttle version of an anti-Aβ antibody, which uses a monovalent binding mode to the TfR, increases β-Amyloid target engagement in a mouse model of Alzheimer's disease by 55-fold compared to the parent antibody. We provide in vitro and in vivo evidence that the monovalent binding mode facilitates transcellular transport, whereas a bivalent binding mode leads to lysosome sorting. Enhanced target engagement of the Brain Shuttle module translates into a significant improvement in amyloid reduction. These findings have major implications for the development of biologics-based treatment of brain disorders.Entities:
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Year: 2014 PMID: 24411731 DOI: 10.1016/j.neuron.2013.10.061
Source DB: PubMed Journal: Neuron ISSN: 0896-6273 Impact factor: 17.173