Carbon nanotubes (CNTs) have attracted great interest of the nano community and beyond. However, the biomedical applications of CNTs arouse serious concerns for their unknown in vivo consequence, in which the information of pharmacokinetics, metabolism and toxicity of CNTs is essential. In this review, we summarize the updated data of CNTs from the biomedical view. The information shows that surface chemistry is crucial in regulating the in vivo behaviors of CNTs. Among the functionalization methods, PEGylation is the most efficient one to improve the pharmacokinetics and biocompatibility of CNTs. The guiding effects of the pharmacokinetics, metabolism and toxicity information on the biomedical applications of CNTs are discussed.

It has been found that the self-assembling peptide RADA 16-I forms a beta-sheet structure and self-assembles into nanofibers and scaffolds in favor of cell growth, hemostasis and tissue-injury repair. But its biophysical and morphological properties, especially for its beta-sheet and self-assembling properties in heat- and pH-denatured conditions, remain largely unclear. In order to better understand and design nanobiomaterials, we studied the self-assembly behaviors of RADA16-I using CD and atomic force microscopy (AFM) measurements in various pH and heat-denatured conditions. Here, we report that the peptide, when exposed to pH 1.0 and 4.0, was still able to assume a typical beta-sheet structure and self-assemble into long nanofiber, although its beta-sheet content was dramatically decreased by 10% in a pH 1.0 solution. However, the peptide, when exposed to pH 13.0, drastically lost its beta-sheet structure and assembled into different small-sized globular aggregates. Similarly, the peptide, when heat-denatured from 25 to 70 degrees C, was still able to assume a typical beta-sheet structure with 46% content, but self-assembled into small-sized globular aggregates at much higher temperature. Titration experiments showed that the peptide RADA16-I exists in three types of ionic species: acidic (fully protonated peptide), zwitterionic (electrically neutral peptide carrying partial positive and negative charges) and basic (fully deprotonated peptide) species, called 'super ions'. The unordered structure and beta-turn of these 'super ions' via hydrogen or ionic bonds, and heat Brownian motion under the above denatured conditions would directly affect the stability of the beta-sheet and nanofibers. These results help us in the design of future nanobiomaterials, such as biosensors, based on beta-sheets and environmental changes. These results also help understand the pathogenesis of the beta-sheet-mediated neuronal diseases such as Alzheimer's disease and the mechanism of hemostasis.

No abstract

A new self-assembling bolaamphiphilic peptide has been designed and synthesized using only natural amino acids. This simple peptide is composed of two lysines connected by 4-8 alanines to maintain the characteristics of the traditional bolaamphiphiles. Based on an irregular secondary structure, it can self-assemble into nanospheres, nanorods, or nanofibers with lengths up to micrometers. The long nanofibers can be broken into smaller fragments by sonication, however, they could reassemble into nanofibers after incubation. Furthermore, the nanostructures were shown to have considerable thermostability. This new bolaamphiphilic peptide differs from any other self-assembling peptides or bolaamphiphiles, and possibly provides a new approach to fabricate nanomaterials.

No abstract