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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Precision Templating with DNA of a Virus-like Particle with Peptide Nanostructures
TL;DR: It is proposed that electrostatic attachment of the nanostructures with sufficiently long PEG segments generates steric forces that increase the rigidity of the neutralized DNA template, which stiffening counterbalances the natural tendency of the DNA template to condense into toroids or buckle multiple times.
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Supramolecular Materials from Triblock Rodcoil Molecules Containing Phenylene Vinylene
TL;DR: In this article, the synthesis and characterization of several triblock rodcoil molecules containing conformationally rigid and flexible sequences and luminescent chromophores based on phenylene vinylene was reported.
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Tunable exciton binding energy in 2D hybrid layered perovskites through donor–acceptor interactions within the organic layer
James V. Passarelli,Catherine M. Mauck,Catherine M. Mauck,Samuel W. Winslow,Collin F. Perkinson,Jacob C. Bard,Hiroaki Sai,Kristopher W. Williams,Ashwin Narayanan,Daniel J. Fairfield,Mark P. Hendricks,William A. Tisdale,Samuel I. Stupp +12 more
TL;DR: Doping two-dimensional naphthalene-based lead halide perovskites with tetrachloro-1,2-benzoquinone has been shown to introduce donor–acceptor interactions within the organic network, without disrupting the inorganic sublattice.
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Electrostatic Control of Bioactivity
TL;DR: The inclusion of charged amino acids in the peptide amphiphiles disrupted the tendency to bundle and led to significantly enhanced neurite outgrowth.
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Self-assembly of biomolecular soft matter
TL;DR: Examples of one-dimensional self-assembly of peptide amphiphiles and the consequent biological functions that emerge in these systems are described.