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@ARTICLE{Elfgen:836466,
author = {Elfgen, Anne and Santiago-Schübel, Beatrix and Gremer,
Lothar and Kutzsche, Janine and Willbold, Dieter},
title = {{S}urprisingly high stability of the {A}β oligomer
eliminating all-d-enantiomeric peptide {D}3 in media
simulating the route of orally administered drugs},
journal = {European journal of pharmaceutical sciences},
volume = {107},
issn = {0928-0987},
address = {New York, NY [u.a.]},
publisher = {Elsevier},
reportid = {FZJ-2017-05584},
pages = {203-207},
year = {2017},
abstract = {The aggregation of the amyloid β protein (Aβ) plays an
important role in the pathology of Alzheimer's disease.
Previously, we have developed the all-d-enantiomeric peptide
D3, which is able to eliminate neurotoxic Aβ oligomers in
vitro and improve cognition in a transgenic Alzheimer's
disease mouse model in vivo even after oral administration.
d-Peptides are expected to be more resistant against
enzymatic proteolysis compared to their l-enantiomeric
equivalents, and indeed, a pharmacokinetic study with
tritiated D3 revealed the oral bioavailability to be about
$58\%.$ To further investigate the underlying properties, we
examined the stability of D3 in comparison to its
corresponding all-l-enantiomeric mirror image l-D3 in media
simulating the gastrointestinal tract, blood and liver.
Potential metabolization was followed by reversed-phase
high-performance liquid chromatography. In simulated gastric
fluid, D3 remained almost completely stable $(89\%)$ within
24 h, while $70\%$ of l-D3 was degraded within the same time
period. Notably, in simulated intestinal fluid, D3 also
remained stable $(96\%)$ for 24 h, whereas l-D3 was
completely metabolized within seconds. In human plasma and
human liver microsomes, l-D3 was metabolized several hundred
times faster than D3. The remarkably high stability may
explain the high oral bioavailability seen in previous
studies allowing oral administration of the drug candidate.
Thus, all-d-enantiomeric peptides may represent a promising
new compound class for drug development.},
cin = {ICS-6 / ZEA-3},
ddc = {610},
cid = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ZEA-3-20090406},
pnm = {553 - Physical Basis of Diseases (POF3-553)},
pid = {G:(DE-HGF)POF3-553},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000407836700020},
pubmed = {pmid:28711713},
doi = {10.1016/j.ejps.2017.07.015},
url = {https://juser.fz-juelich.de/record/836466},
}