RT Journal Article
SR Electronic
T1 Simple and highly efficient detection of PSD95 using a nanobody and its recombinant minibody derivative
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2023.03.16.532938
DO 10.1101/2023.03.16.532938
A1 Markus Kilisch
A1 Maja Gere-Becker
A1 Liane Wüstefeld
A1 Christel Bonnas
A1 Alexander Crauel
A1 Maja Mechmershausen
A1 Henrik Martens
A1 Hansjörg Götzke
A1 Felipe Opazo
A1 Steffen Frey
YR 2023
UL http://biorxiv.org/content/early/2023/03/17/2023.03.16.532938.abstract
AB The post-synaptic density protein 95 (PSD95) is a crucial scaffolding protein participating in the organization and regulation of synapses. PSD95 interacts with numerous molecules, including neurotransmitter receptors and ion channels. The functional dysregulation of PSD95 as well as its abundance and localization has been implicated with several neurological disorders, making it an attractive target to develop strategies able to monitor PSD95 accurately for diagnostics and therapeutics. This study characterizes a novel camelid single-domain antibody (nanobody) that binds strongly and with high specificity to rat, mouse and human PSD95. This nanobody allows for a more precise detection and better quantification of PSD95 in various biological samples. We expect that the flexibility and unique performance of this thoroughly characterized affinity tool will help to further understand the role of PSD95 in normal and diseased neuronal synapses.Competing Interest StatementAuthors of this manuscript are employees or shareholders of NanoTag Biotechnologies GmbH or Synaptic Systems GmbH.