We present a generalized table of extinction coefficient data for silver nanoparticles from 8 to 100 nm. This table allows for easy and quick estimation of the concentration and size of modified and mono-dispersed silver nanoparticles from their optical spectra. We obtained data by determining the silver content of citrate-stabilised silver nanoparticles using sodium cyanide to dissolve the nanoparticles, and measuring solution conductivity with a pH meter and a cyanide-ion selective electrode. The quantification of the silver ion concentration enabled the calculation of extinction coefficients. Experimentally calculated extinction coefficients, in the current work, are in good agreement with collated literature values measured by different authors with non-standardized methodology and each for a limited range of particle size. They are also in good agreement with our theoretical calculations using Mie theory. Thus, we provide a highly standardized and comprehensive tabulated reference data-set.

A large body of evidence supports the involvement of heparan sulfate (HS) proteoglycans in physiological processes such as development and diseases including cancer and neurodegenerative disorders. The role of HS emerges from its ability to interact and regulate the activity of a vast number of extracellular proteins including growth factors and extracellular matrix components. A global view on how protein-HS interactions influence the extracellular proteome and, consequently, cell function is currently lacking. Here, we systematically investigate the functional and structural properties that characterize HS-interacting proteins and the network they form. We collected 435 human proteins interacting with HS or the structurally related heparin by integrating literature-derived and affinity proteomics data. We used this data set to identify the topological features that distinguish the heparin/HS-interacting network from the rest of the extracellular proteome and to analyze the enrichment of gene ontology terms, pathways, and domain families in heparin/HS-binding proteins. Our analysis revealed that heparin/HS-binding proteins form a highly interconnected network, which is functionally linked to physiological and pathological processes that are characteristic of higher organisms. Therefore, we then investigated the existence of a correlation between the expansion of domain families characteristic of the heparin/HS interactome and the increase in biological complexity in the metazoan lineage. A strong positive correlation between the expansion of the heparin/HS interactome and biosynthetic machinery and organism complexity emerged. The evolutionary role of HS was reinforced by the presence of a rudimentary HS biosynthetic machinery in a unicellular organism at the root of the metazoan lineage.