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Single Amino Acid Modifications for Controlling the Helicity of Peptide-Based Chiral Gold Nanoparticle Superstructures.
Brooks, Sydney C; Jin, Ruitao; Zerbach, Victoria C; Zhang, Yuyu; Walsh, Tiffany R; Rosi, Nathaniel L.
Afiliación
  • Brooks SC; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
  • Jin R; Institute for Frontier Materials, Deakin University, Geelong, Victoria 3216, Australia.
  • Zerbach VC; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
  • Zhang Y; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
  • Walsh TR; Institute for Frontier Materials, Deakin University, Geelong, Victoria 3216, Australia.
  • Rosi NL; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
J Am Chem Soc ; 145(11): 6546-6553, 2023 03 22.
Article en En | MEDLINE | ID: mdl-36912863
Assembling nanoparticles (NPs) into well-defined superstructures can lead to emergent collective properties that depend on their 3-D structural arrangement. Peptide conjugate molecules designed to both bind to NP surfaces and direct NP assembly have proven useful for constructing NP superstructures, and atomic- and molecular-level alterations to these conjugates have been shown to manifest in observable changes to nanoscale structure and properties. The divalent peptide conjugate, C16-(PEPAu)2 (PEPAu = AYSSGAPPMPPF), directs the formation of one-dimensional helical Au NP superstructures. This study examines how variation of the ninth amino acid residue (M), which is known to be a key Au anchoring residue, affects the structure of the helical assemblies. A series of conjugates of differential Au binding affinities based on variation of the ninth residue were designed, and Replica Exchange with Solute Tempering (REST) Molecular Dynamics simulations of the peptides on an Au(111) surface were performed to determine the approximate surface contact and to assign a binding score for each new peptide. A helical structure transition from double helices to single helices is observed as the peptide binding affinity to the Au(111) surface decreases. Accompanying this distinct structural transition is the emergence of a plasmonic chiroptical signal. REST-MD simulations were also used to predict new peptide conjugate molecules that would preferentially direct the formation of single-helical AuNP superstructures. Significantly, these findings demonstrate how small modifications to peptide precursors can be leveraged to precisely direct inorganic NP structure and assembly at the nano- and microscale, further expanding and enriching the peptide-based molecular toolkit for controlling NP superstructure assembly and properties.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Nanopartículas del Metal / Oro Tipo de estudio: Prognostic_studies Idioma: En Revista: J Am Chem Soc Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Nanopartículas del Metal / Oro Tipo de estudio: Prognostic_studies Idioma: En Revista: J Am Chem Soc Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos