A database on the stability of silver and gold nanostructures for applications in biology and biomolecular sciences.

Colloidal stability of nanoparticles in biological media is an important consideration when trying to ensure reliable data interpretation of in vitro and in vivo systems. We have developed a detailed colloidal stability library of newly synthesized gold, silver and gold-core silver-shell plasmonic nanoparticles, stabilized with aspartame, glucosamine and sucralose, in various biologically relevant buffers and bacterial and mammalian cell culture media. The stabilizer selection reflects the preference for molecules that are non-toxic, inexpensive, readily available, water soluble and easy-to-replace if that is the end-user preference. An on-line resource provides detailed stability information on each of the 81 systems examined. To illustrate how to utilize this stability library, we conducted bacterial toxicity and biocompatibility experiments through the use of one specific set of nanomaterials in the presence and absence of plasmonic irradiation.

Binding of [Cr(phen)3](3+) to transferrin at extracellular and endosomal pHs: potential application in photodynamic therapy.

BACKGROUND: Transferrin is an iron-binding blood plasma glycoprotein that controls the level of free iron in biological fluids. This protein has been deeply studied in the past few years because of its potential use as a strategy of drug targeting to tumor tissues. Chromium complex, [Cr(phen)3](3+) (phen=1,10-phenanthroline), has been proposed as photosensitizers for photodynamic therapy (PDT). Thus, we analyzed the binding of chromium complex, [Cr(phen)3](3+), to transferrin for a potential delivery of this diimine complex to tumor cells for PDT. METHODS: The interaction between [Cr(phen)3](3+) and holotransferrin (holoTf) was studied by fluorescence quenching technique, circular dichroism (CD) and ultraviolet (UV)-visible spectroscopy. RESULTS: [Cr(phen)3](3+) binds strongly to holoTf with a binding constant around 10(5)M(-1), that depends on the pH. The thermodynamic parameters indicated that hydrophobic interactions played a major role in the binding processes. The CD studies showed that there are no conformational changes in the secondary and tertiary structures of the protein. CONCLUSIONS: These results suggest that the binding process would occur in a site different from the specific iron binding sites of the protein and would be the same in both protein states. As secondary and tertiary structures of transferrin do not show remarkable changes, we propose that the TfR could recognize the holoTf despite having a chromium complex associated. GENERAL SIGNIFICANCE: Understanding the interaction between [Cr(phen)3](3+) with transferrin is relevant because this protein could be a delivery agent of Cr(III) complex to tumor cells. This can allow us to understand further the role of Cr(III) complex as sensitizer in PDT.