Advanced Functional Materials · 2011 · 76 citations · 78 references
Life SciencesBiochemistryMaterials ScienceBiomaterialsNanobiotechnologyNanomaterialsAmino Acid ChemistryAmyloid FormationMacromolecular AssemblyNanomedicineNanoparticle DesignNanoparticle StabilityAmino AcidsAmyloid Fibril FormationAmyloid FibrilsAmyloid NanostructuresNanoparticlesProteolytic StabilitySolvent PolarityThermal Stability
Abstract The small‐sized molecules that have been developed from single hydrophobic amino acids (Phe, Trp, Tyr and Leu) by suitably protecting the –NH 2 and –CO 2 H groups generate diverse nanoscopic structures – such as nanorods, nanofibrils, nanotubes, and nanovesicles – depending upon the protection parameters and solvent polarity. The vesicular structures get disrupted in the presence of various salts, such as KCl, CaCl 2 , (NH 4 ) 2 SO 4 and N(n‐Bu) 4 Br. Insertion of unnatural ( o / m / p )‐aminobenzoic acids as a protecting group and the lack of conventional peptide bonds in the molecules give the nanostructures proteolytic stability. The nanostructures also show significant thermal stability along with a morphological transformation upon heat treatment. Our in vitro studies reveal that the addition of micromolar concentration “curcumin” significantly reduces the formation of amyloid‐like fibrils. These diverse nanostructures are used as a template for fabricating silver nanoparticles on their outer surfaces as well as in the inner part, followed by calcination in air which helps to obtain a 1D silver nanostructure. Furthermore, the nanovesicles are observed to encapsulate a potent drug (curcumin) and other biologically important molecules, which could be released through salt‐triggered disruption of vesicles.
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