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A disintegrin derivative as a case study for PHIP labeling of disulfide bridged biomolecules

Fleckenstein, Max ; Herr, Kevin Sebastian ; Theiß, Franziska ; Knecht, Stephan ; Wienands, Laura ; Brodrecht, Martin ; Reggelin, Michael ; Buntkowsky, Gerd (2022)
A disintegrin derivative as a case study for PHIP labeling of disulfide bridged biomolecules.
In: Scientific Reports, 2022, 12
doi: 10.26083/tuprints-00021461
Article, Secondary publication, Publisher's Version

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Item Type: Article
Type of entry: Secondary publication
Title: A disintegrin derivative as a case study for PHIP labeling of disulfide bridged biomolecules
Language: English
Date: 7 June 2022
Place of Publication: Darmstadt
Year of primary publication: 2022
Publisher: Springer Nature
Journal or Publication Title: Scientific Reports
Volume of the journal: 12
Collation: 8 Seiten
DOI: 10.26083/tuprints-00021461
Corresponding Links:
Origin: Secondary publication via sponsored Golden Open Access
Abstract:

A specific labeling strategy for bioactive molecules is presented for eptifibatide (integrilin) an antiplatelet aggregation inhibitor, which derives from the disintegrin protein barbourin in the venom of certain rattlesnakes. By specifically labeling the disulfide bridge this molecule becomes accessible for the nuclear spin hyperpolarization method of parahydrogen induced polarization (PHIP). The PHIP-label was synthesized and inserted into the disulfide bridge of eptifibatide via reduction of the peptide and insertion by a double Michael addition under physiological conditions. This procedure is universally applicable for disulfide-containing biomolecules and preserves their tertiary structure with a minimum of change. HPLC and MS spectra prove the successful insertion of the label. 1H-PHIP-NMR experiments yield a factor of over 1000 as lower limit for the enhancement factor. These results demonstrate the high potential of the labeling strategy for the introduction of site selective PHIP-labels into biomolecules’ disulfide bonds.

Status: Publisher's Version
URN: urn:nbn:de:tuda-tuprints-214619
Additional Information:

Keywords: Biophysical chemistry, chemical physics, peptides

Classification DDC: 500 Science and mathematics > 540 Chemistry
Divisions: 07 Department of Chemistry > Clemens-Schöpf-Institut > Organ Chemistry
07 Department of Chemistry > Eduard Zintl-Institut > Physical Chemistry
Date Deposited: 07 Jun 2022 12:09
Last Modified: 06 Dec 2023 08:41
URI: https://tuprints.ulb.tu-darmstadt.de/id/eprint/21461
PPN: 495283320
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