이성수 (Northwestern University, 현 Stanford University)

한빛사논문

조회1,452

Northwestern University, 현 Stanford University

Nat. Nanotechnol., Published online 19 June 2017 | doi:10.1038/nnano.2017.109 Sulfated glycopeptide nanostructures for multipotent protein activation

Sungsoo S. Lee^1,2†‡, Timmy Fyrner^1‡, Feng Chen¹, Zaida Alvarez¹, Eduard Sleep¹, Danielle S. Chun³, Joseph A. Weiner³, Ralph W. Cook³, Ryan D. Freshman³, Michael S. Schallmo³, Karina M. Katchko³, Andrew D. Schneider³, Justin T. Smith³, Chawon Yun³, Gurmit Singh³, Sohaib Z. Hashmi³, Mark T. McClendon¹, Zhilin Yu¹, Stuart R. Stock⁴, Wellington K. Hsu^1,3, Erin L. Hsu^1,3 and Samuel I. Stupp^1,2,5,6,7*¹Simpson Querrey Institute for BioNanotechnology, Northwestern University, Chicago, Illinois 60611, USA. ²Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, USA. ³Department of Orthopaedic Surgery, Northwestern University, Chicago, Illinois 60208, USA. ⁴Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, Illinois 60611, USA. ⁵Department of Biomedical Engineering, Northwestern University, Evanston, Illinois 60208, USA. ⁶Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA. ⁷Department of Medicine, Northwestern University, Chicago, Illinois 60611, USA. ^†Present address: Blau Laboratory, Baxter Laboratory for Stem Cell Biology, Stanford University School of Medicine, Stanford, California 94305, USA. ^‡These authors contributed equally to this work.

Correspondence to : Samuel I. Stupp

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.

논문정보

형식Research article
게재일2017년 06월 (BRIC 등록일 2017-06-21)
연구진국외 연구진
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