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Title: Sulfated glycopeptide nanostructures for multipotent protein activation

Abstract

Biological systems have evolved to utilize numerous proteins with capacity to bind polysaccharides for the purpose of optimizing their function. A well-known subset of these proteins with binding domains for the highly diverse sulfated polysaccharides are important growth factors involved in biological development and tissue repair. We report here on supramolecular sulfated glycopeptide nanostructures, which display a trisulfated monosaccharide on their surfaces and bind five critical proteins with different polysaccharide-binding domains. Binding does not disrupt the filamentous shape of the nanostructures or their internal β-sheet backbone, but must involve accessible adaptive configurations to interact with such different proteins. The glycopeptide nanostructures amplified signalling of bone morphogenetic protein 2 significantly more than the natural sulfated polysaccharide heparin, and promoted regeneration of bone in the spine with a protein dose that is 100-fold lower than that required in the animal model. These highly bioactive nanostructures may enable many therapies in the future involving proteins.

Authors:
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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1375354
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature Nanotechnology; Journal Volume: 12; Journal Issue: 8
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Lee, Sungsoo S., Fyrner, Timmy, Chen, Feng, Álvarez, Zaida, Sleep, Eduard, Chun, Danielle S., Weiner, Joseph A., Cook, Ralph W., Freshman, Ryan D., Schallmo, Michael S., Katchko, Karina M., Schneider, Andrew D., Smith, Justin T., Yun, Chawon, Singh, Gurmit, Hashmi, Sohaib Z., McClendon, Mark T., Yu, Zhilin, Stock, Stuart R., Hsu, Wellington K., Hsu, Erin L., and Stupp, Samuel I.. Sulfated glycopeptide nanostructures for multipotent protein activation. United States: N. p., 2017. Web. doi:10.1038/nnano.2017.109.
Lee, Sungsoo S., Fyrner, Timmy, Chen, Feng, Álvarez, Zaida, Sleep, Eduard, Chun, Danielle S., Weiner, Joseph A., Cook, Ralph W., Freshman, Ryan D., Schallmo, Michael S., Katchko, Karina M., Schneider, Andrew D., Smith, Justin T., Yun, Chawon, Singh, Gurmit, Hashmi, Sohaib Z., McClendon, Mark T., Yu, Zhilin, Stock, Stuart R., Hsu, Wellington K., Hsu, Erin L., & Stupp, Samuel I.. Sulfated glycopeptide nanostructures for multipotent protein activation. United States. doi:10.1038/nnano.2017.109.
Lee, Sungsoo S., Fyrner, Timmy, Chen, Feng, Álvarez, Zaida, Sleep, Eduard, Chun, Danielle S., Weiner, Joseph A., Cook, Ralph W., Freshman, Ryan D., Schallmo, Michael S., Katchko, Karina M., Schneider, Andrew D., Smith, Justin T., Yun, Chawon, Singh, Gurmit, Hashmi, Sohaib Z., McClendon, Mark T., Yu, Zhilin, Stock, Stuart R., Hsu, Wellington K., Hsu, Erin L., and Stupp, Samuel I.. Mon . "Sulfated glycopeptide nanostructures for multipotent protein activation". United States. doi:10.1038/nnano.2017.109.
@article{osti_1375354,
title = {Sulfated glycopeptide nanostructures for multipotent protein activation},
author = {Lee, Sungsoo S. and Fyrner, Timmy and Chen, Feng and Álvarez, Zaida and Sleep, Eduard and Chun, Danielle S. and Weiner, Joseph A. and Cook, Ralph W. and Freshman, Ryan D. and Schallmo, Michael S. and Katchko, Karina M. and Schneider, Andrew D. and Smith, Justin T. and Yun, Chawon and Singh, Gurmit and Hashmi, Sohaib Z. and McClendon, Mark T. and Yu, Zhilin and Stock, Stuart R. and Hsu, Wellington K. and Hsu, Erin L. and Stupp, Samuel I.},
abstractNote = {Biological systems have evolved to utilize numerous proteins with capacity to bind polysaccharides for the purpose of optimizing their function. A well-known subset of these proteins with binding domains for the highly diverse sulfated polysaccharides are important growth factors involved in biological development and tissue repair. We report here on supramolecular sulfated glycopeptide nanostructures, which display a trisulfated monosaccharide on their surfaces and bind five critical proteins with different polysaccharide-binding domains. Binding does not disrupt the filamentous shape of the nanostructures or their internal β-sheet backbone, but must involve accessible adaptive configurations to interact with such different proteins. The glycopeptide nanostructures amplified signalling of bone morphogenetic protein 2 significantly more than the natural sulfated polysaccharide heparin, and promoted regeneration of bone in the spine with a protein dose that is 100-fold lower than that required in the animal model. These highly bioactive nanostructures may enable many therapies in the future involving proteins.},
doi = {10.1038/nnano.2017.109},
journal = {Nature Nanotechnology},
number = 8,
volume = 12,
place = {United States},
year = {Mon Jun 19 00:00:00 EDT 2017},
month = {Mon Jun 19 00:00:00 EDT 2017}
}