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.

Bibliographic Details
Main Authors: Alessandro Zorzi, Simon J. Middendorp, Jonas Wilbs, Kaycie Deyle, Christian Heinis
Format: Article
Language:English
Published: Nature Publishing Group 2017-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms16092
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spelling 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
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