Sulfated glycopeptide nanostructures for multipotent protein activation

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.

doi:10.1038/NNANO.2017.109

Title: Sulfated glycopeptide nanostructures for multipotent protein activation

Journal Article · Mon Jun 19 00:00:00 EDT 2017 · Nature Nanotechnology

DOI:https://doi.org/10.1038/NNANO.2017.109· OSTI ID:1463097

Lee, Sungsoo S. ^[1]; Fyrner, Timmy ^[2]; Chen, Feng ^[2]; Álvarez, Zaida ^[2]; Sleep, Eduard ^[2]; Chun, Danielle S. ^[3]; Weiner, Joseph A. ^[3]; Cook, Ralph W. ^[3]; Freshman, Ryan D. ^[3]; Schallmo, Michael S. ^[3]; Katchko, Karina M. ^[3]; Schneider, Andrew D. ^[3]; Smith, Justin T. ^[3]; Yun, Chawon ^[3]; Singh, Gurmit ^[3]; Hashmi, Sohaib Z. ^[3]; McClendon, Mark T. ^[2]; Yu, Zhilin ^[2]; Stock, Stuart R. ^[4]; Hsu, Wellington K. ^[5] more »

Stanford Univ., CA (United States). School of Medicine, Blau Lab., and Baxter Lab. for Stem Cell Biology; Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology and Dept. of Materials Science and Engineering
Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology
Northwestern Univ., Evanston, IL (United States). Dept. of Orthopaedic Surgery
Northwestern Univ., Evanston, IL (United States). Dept. of Molecular Pharmacology and Biological Chemistry
Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology and Dept. of Orthopaedic Surgery
Northwestern Univ., Evanston, IL (United States). Simpson Querrey Inst. for BioNanotechnology, Dept. of Materials Science and Engineering, Dept. of Biomedical Engineering, Dept. of Chemistry and Dept. of Medicine

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. Here, we report on supramolecular sulfated glycopeptide nanostructures, which display a trisulfated monosaccharide on their surfaces and bind five critical proteins with very 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 signaling 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 expected. These super-bioactive nanostructures may enable many therapies in the horizon involving proteins.

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Research Organization:: Energy Frontier Research Centers (EFRC) (United States). Center for Bio-Inspired Energy Science (CBES); Northwestern Univ., Evanston, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); Samsung Scholarship

Contributing Organization:: Argonne National Laboratory (ANL); Univ. of Chicago; Würzburg Univ.; Univ. of California; Washington Univ.

Grant/Contract Number:: SC0000989; 5R01DE015920-10; FG02-00ER45810

OSTI ID:: 1463097

Alternate ID(s):: OSTI ID: 1821867; OSTI ID: 1846931

Journal Information:: Nature Nanotechnology, Vol. 12, Issue 8; ISSN 1748-3387

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 119 works

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