Multi-site esterification: a tunable, reversible strategy to tailor therapeutic peptides for delivery-Reference-Cited by-同舟云学术

Multi-site esterification: a tunable, reversible strategy to tailor therapeutic peptides for delivery

Published:2024 Issue: Volume: Page:
ISSN:2058-9689
Container-title:Molecular Systems Design & Engineering
language:en
Short-container-title:Mol. Syst. Des. Eng.

Author:

Bannon Mark S.¹^ORCID,Ellena Jeffrey F.²,Gourishankar Aditi S.¹,Marsh Spencer R.³^ORCID,Trevisan-Silva Dilza⁴,Sherman Nicholas E.⁴^ORCID,Jourdan L. Jane³,Gourdie Robert G.³,Letteri Rachel A.¹^ORCID

Affiliation:

1. Department of Chemical Engineering, University of Virginia, Charlottesville, VA, 22903, USA

2. Biomolecular Magnetic Resonance Facility, School of Medicine, University of Virginia, Charlottesville, VA, 22903, USA

3. Fralin Biomedical Institute, Virginia Tech Carillion School of Medicine, Roanoke, VA, 24016, USA

4. Biomolecular Analysis Facility, School of Medicine, University of Virginia, Charlottesville, VA, 22903, USA

Abstract

Peptides are naturally potent and selective therapeutics with massive potential; however, low cell membrane permeability limits their clinical implementation, particularly for hydrophilic, anionic peptides with intracellular targets.

Funder

National Institute of General Medical Sciences

Small Business Innovative Research and Small Business Technology Transfer

National Heart, Lung, and Blood Institute

Virginia Biosciences Health Research Corporation

National Science Foundation

School of Engineering and Applied Science, University of Virginia

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/ME/D4ME00072B

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