S
Samuel I. Stupp
Researcher at Northwestern University
Publications - 587
Citations - 54611
Samuel I. Stupp is an academic researcher from Northwestern University. The author has contributed to research in topics: Peptide amphiphile & Supramolecular chemistry. The author has an hindex of 109, co-authored 560 publications receiving 49166 citations. Previous affiliations of Samuel I. Stupp include Urbana University & Max Planck Society.
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Semiconductor nanohelices templated by supramolecular ribbons.
TL;DR: Nanohelices of cadmium sulfide (CdS) have been made by the mineralization of supramolecular organic ribbons by growth along one face of the ribbon.
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Bone regeneration mediated by biomimetic mineralization of a nanofiber matrix.
Alvaro Mata,Yanbiao Geng,Karl Henrikson,Conrado Aparicio,Stuart R. Stock,Robert L. Satcher,Robert L. Satcher,Samuel I. Stupp +7 more
TL;DR: The use of self-assembling peptide nanostructured gels to promote bone regeneration that have the capacity to mineralize in biomimetic fashion is reported on.
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Synthesis, self-assembly, and characterization of supramolecular polymers from electroactive dendron rodcoil molecules.
TL;DR: Electron and atomic force microscopy reveals the self-assembly of the molecules into high aspect ratio ribbon-like nanostructures which at low concentrations induce gelation in nonpolar solvent and electric field alignment of these supramolecular assemblies can be used to create arrays of self-assembled nanowires on a device substrate.
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Bone regeneration with low dose BMP-2 amplified by biomimetic supramolecular nanofibers within collagen scaffolds
Sungsoo S. Lee,Brian J. Huang,Stuart R. Kaltz,Shantanu Sur,Christina J. Newcomb,Stuart R. Stock,Ramille N. Shah,Samuel I. Stupp +7 more
TL;DR: A synthetic biomimetic strategy that emulates biological BMP-2 signaling through the use of peptide amphiphile nanofibers designed to bind heparin is reported on, demonstrating how molecularly designed materials that mimic features of the extracellular environment can amplify the regenerative capacity of growth factors.
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Amino acid sequence in constitutionally isomeric tetrapeptide amphiphiles dictates architecture of one-dimensional nanostructures.
TL;DR: The use of isomeric peptide amphiphiles as molecular building blocks to create one-dimensional (1D) nanostructures is reported to demonstrate the significance of peptide side chain interactions in determining the architectures of supramolecular assemblies.