A nanostructured carbon-reinforced polyisobutylene-based thermoplastic elastomer.

This paper presents the synthesis and characterization of a polyisobutylene (PIB)-based nanostructured carbon-reinforced thermoplastic elastomer. This thermoplastic elastomer is based on a self-assembling block copolymer having a branched PIB core carrying -OH functional groups at each branch point, flanked by blocks of poly(isobutylene-co-para-methylstyrene). The block copolymer has thermolabile physical crosslinks and can be processed as a plastic, yet retains its rubbery properties at room temperature. The carbon-reinforced thermoplastic elastomer had more than twice the tensile strength of the neat polymer, exceeding the strength of medical grade silicone rubber, while remaining significantly softer. The carbon-reinforced thermoplastic elastomer displayed a high T(g) of 126 degrees C, rendering the material steam-sterilizable. The carbon also acted as a free radical trap, increasing the onset temperature of thermal decomposition in the neat polymer from 256.6 degrees C to 327.7 degrees C. The carbon-reinforced thermoplastic elastomer had the lowest water contact angle at 82 degrees and surface nano-topography. After 180 days of implantation into rabbit soft tissues, the carbon-reinforced thermoplastic elastomer had the thinnest tissue capsule around the microdumbbell specimens, with no eosinophiles present. The material also showed excellent integration into bones.

The effects of three Drosophila melanogaster myotropins on the frequency of foregut contractions differ.

Myotropic peptides can be grouped into different families based on their structure. Three Drosophila melanogaster myotropin families are represented by TDVDHVFLRFamide, dromyosuppressin (DMS), pEVRYRQCYFNPISCF, an allatostatin C-type peptide named flatline (FLT), and SDNFMRFamide, a FMRFamide-containing peptide. The structures of DMS, FLT, and SDNFMRFamide differ and each peptide is encoded by a different gene. In addition, the spatial and temporal distributions of DMS, FLT, and SDNFMRFamide are dissimilar. DMS, FLT, and SDNFMRFamide each decreases heart rate; however, their effects are profoundly different. Likewise, the effects of these three myotropins on the frequency of the spontaneous contractions of the crop, an anterior portion of the foregut, differ. DMS stops crop movement without recovery for at least a 10-min period after applying the peptide, FLT significantly decreases the frequency of spontaneous contractions, but its effect partially reverses within a few minutes after applying the peptide, and SDNFMRFamide only slightly decreased crop motility, an effect that was not significantly different from the effect of saline. The differences in the structures, distributions, and activities of DMS, FLT, and SDNFMRFamide suggest their synthesis and release are under different sensory inputs and regulatory mechanisms, and that roles in affecting the frequency of crop contractions differ.