Characterization of the PEGylated Functional Upstream Domain Peptide (PEG-FUD): a Potent Fibronectin Assembly Inhibitor with Potential as an Anti-Fibrotic Therapeutic

Characterization of the PEGylated Functional Upstream Domain Peptide (PEG-FUD): a Potent... Pharm Res (2018) 35: 126 https://doi.org/10.1007/s11095-018-2412-7 RESEARCH PAPER Characterization of the PEGylated Functional Upstream Domain Peptide (PEG-FUD): a Potent Fibronectin Assembly Inhibitor with Potential as an Anti-Fibrotic Therapeutic 1 1 2 1 Pawel Zbyszynski & Bianca R. Tomasini-Johansson & Donna M. Peters & Glen S. Kwon Received: 17 March 2018 /Accepted: 17 April 2018 /Published online: 24 April 2018 # Springer Science+Business Media, LLC, part of Springer Nature 2018 ABSTRACT that PEG-FUD holds promise as an effective anti-fibrotic with Purpose To develop PEGylated variants of pUR4/FUD therapeutic potential and a candidate for further pharmaco- (FUD), a fibronectin assembly inhibitor, using 10 kDa, kinetic and biodistribution studies. 20 kDa, and 40 kDa PEGs to evaluate their binding affinity and inhibitory potency. . . . KEYWORDS Anti-fibrosis therapy fibronectin PEG Methods The FUD peptide was recombinantly expressed, peptide delivery pUR4/FUD purified, and PEGylated at the N-terminus using 10 kDa, 20 kDa, and 40 kDa methoxy-PEG aldehyde. The PEGylates were purified and fractionated using ion- ABBREVIATIONS exchange chromatography. The molecular weight and degree 70 K 70 kDa N-terminal region of fibronectin of PEGylation of each conjugate was verified using MALDI- ECM Extracellular Matrix TOF. The binding affinity of each PEG-FUD conjugate was http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Pharmaceutical Research Springer Journals

Characterization of the PEGylated Functional Upstream Domain Peptide (PEG-FUD): a Potent Fibronectin Assembly Inhibitor with Potential as an Anti-Fibrotic Therapeutic

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Publisher
Springer US
Copyright
Copyright © 2018 by Springer Science+Business Media, LLC, part of Springer Nature
Subject
Biomedicine; Pharmacology/Toxicology; Pharmacy; Biochemistry, general; Medical Law; Biomedical Engineering
ISSN
0724-8741
eISSN
1573-904X
D.O.I.
10.1007/s11095-018-2412-7
Publisher site
See Article on Publisher Site

Abstract

Pharm Res (2018) 35: 126 https://doi.org/10.1007/s11095-018-2412-7 RESEARCH PAPER Characterization of the PEGylated Functional Upstream Domain Peptide (PEG-FUD): a Potent Fibronectin Assembly Inhibitor with Potential as an Anti-Fibrotic Therapeutic 1 1 2 1 Pawel Zbyszynski & Bianca R. Tomasini-Johansson & Donna M. Peters & Glen S. Kwon Received: 17 March 2018 /Accepted: 17 April 2018 /Published online: 24 April 2018 # Springer Science+Business Media, LLC, part of Springer Nature 2018 ABSTRACT that PEG-FUD holds promise as an effective anti-fibrotic with Purpose To develop PEGylated variants of pUR4/FUD therapeutic potential and a candidate for further pharmaco- (FUD), a fibronectin assembly inhibitor, using 10 kDa, kinetic and biodistribution studies. 20 kDa, and 40 kDa PEGs to evaluate their binding affinity and inhibitory potency. . . . KEYWORDS Anti-fibrosis therapy fibronectin PEG Methods The FUD peptide was recombinantly expressed, peptide delivery pUR4/FUD purified, and PEGylated at the N-terminus using 10 kDa, 20 kDa, and 40 kDa methoxy-PEG aldehyde. The PEGylates were purified and fractionated using ion- ABBREVIATIONS exchange chromatography. The molecular weight and degree 70 K 70 kDa N-terminal region of fibronectin of PEGylation of each conjugate was verified using MALDI- ECM Extracellular Matrix TOF. The binding affinity of each PEG-FUD conjugate was

Journal

Pharmaceutical ResearchSpringer Journals

Published: Apr 24, 2018

References

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