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• W2040802180 endingPage "2223" @default.
• W2040802180 startingPage "2218" @default.
• W2040802180 abstract "Biologically templated nanoparticles are of interest for a variety of biological applications and for controlling the porosity and other properties in nanocomposites. Solid-state NMR has been used to characterize polypeptide/silica composites templated from the poly(l-lysine) solutions in the α-helix, β-sheet, and random coil conformations. The results show that the poly(l-lysine) retains its solution conformation in the nanocomposites when templating from the α-helix or β-sheet conformation, but the random coil conformation is partially converted to the α-helical form during nanocomposite formation. The dynamics of poly(l-lysine) are restricted by incorporation into the composite compared to bulk poly(l-lysine) at the equivalent relative humidity. Bulk and film poly(l-lysine) samples undergo transitions from the random coil to the β-sheet to the α-helix conformation with increasing relative humidity, but these transitions are suppressed in the silica composite. {1H-31P} NMR studies show that inorganic phosphate is incorporated into the random coil-templated composite and that part of the phosphate is closely associated with the poly(l-lysine). The implications for biomimetic nanocomposites formation are considered." @default.
• W2040802180 created "2016-06-24" @default.
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• W2040802180 date "2008-02-19" @default.
• W2040802180 modified "2023-09-30" @default.
• W2040802180 title "The Structure and Dynamics of Poly(<scp>l</scp>-lysine) in Templated Silica Nanocomposites" @default.
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• W2040802180 doi "https://doi.org/10.1021/cm702283u" @default.
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