Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides
A major challenge for the application of peptide therapeutics is their short half-lifein vivo. Here, the authors design peptide-fatty acid chimeras bearing an engineered linker that promotes albumin binding and allows longer circulation times of therapeutic peptides in animal models.
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Nature Publishing Group
2017-07-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms16092 |
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doaj-cb4c3effd8b24083a11b07d420333e2b2021-05-11T07:44:06ZengNature Publishing GroupNature Communications2041-17232017-07-01811910.1038/ncomms16092Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptidesAlessandro Zorzi0Simon J. Middendorp1Jonas Wilbs2Kaycie Deyle3Christian Heinis4Institute of Chemical Sciences and Engineering, School of Basic Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)Institute of Chemical Sciences and Engineering, School of Basic Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)Institute of Chemical Sciences and Engineering, School of Basic Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)Institute of Chemical Sciences and Engineering, School of Basic Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)Institute of Chemical Sciences and Engineering, School of Basic Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)A major challenge for the application of peptide therapeutics is their short half-lifein vivo. Here, the authors design peptide-fatty acid chimeras bearing an engineered linker that promotes albumin binding and allows longer circulation times of therapeutic peptides in animal models.https://doi.org/10.1038/ncomms16092 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Alessandro Zorzi Simon J. Middendorp Jonas Wilbs Kaycie Deyle Christian Heinis |
spellingShingle |
Alessandro Zorzi Simon J. Middendorp Jonas Wilbs Kaycie Deyle Christian Heinis Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides Nature Communications |
author_facet |
Alessandro Zorzi Simon J. Middendorp Jonas Wilbs Kaycie Deyle Christian Heinis |
author_sort |
Alessandro Zorzi |
title |
Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides |
title_short |
Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides |
title_full |
Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides |
title_fullStr |
Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides |
title_full_unstemmed |
Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides |
title_sort |
acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2017-07-01 |
description |
A major challenge for the application of peptide therapeutics is their short half-lifein vivo. Here, the authors design peptide-fatty acid chimeras bearing an engineered linker that promotes albumin binding and allows longer circulation times of therapeutic peptides in animal models. |
url |
https://doi.org/10.1038/ncomms16092 |
work_keys_str_mv |
AT alessandrozorzi acylatedheptapeptidebindsalbuminwithhighaffinityandapplicationastagfurnisheslongactingpeptides AT simonjmiddendorp acylatedheptapeptidebindsalbuminwithhighaffinityandapplicationastagfurnisheslongactingpeptides AT jonaswilbs acylatedheptapeptidebindsalbuminwithhighaffinityandapplicationastagfurnisheslongactingpeptides AT kayciedeyle acylatedheptapeptidebindsalbuminwithhighaffinityandapplicationastagfurnisheslongactingpeptides AT christianheinis acylatedheptapeptidebindsalbuminwithhighaffinityandapplicationastagfurnisheslongactingpeptides |
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