-(Hydroxybenzyl)benzamide Derivatives: Aqueous pH-Dependent Kinetics and Mechanistic Implications for the Aqueous Reactivity of Carbinolamides.

The rate constants for the aqueous reaction, between pH 0 and 14, have been determined for a series of amide substituted -(hydroxybenzyl)benzamide derivatives, in HO, at 25 °C, = 1.0 M (KCl). The -(hydroxybenzyl)benzamide derivatives were found to react via three distinct mechanisms with the kinetically dominant mechanism being dependent on the pH of the reaction solution.

The effect of three different (-135°C) whole body cryotherapy exposure durations on elite rugby league players.

Background: Whole body cryotherapy (WBC) is the therapeutic application of extreme cold air for a short duration. Minimal evidence is available for determining optimal exposure time.

Purpose: To explore whether the length of WBC exposure induces differential changes in inflammatory markers, tissue oxygenation, skin and core temperature, thermal sensation and comfort.

Hierarchical assembly of collagen peptide triple helices into curved disks and metal ion-promoted hollow spheres.

A 27 amino acid collagen-based peptide (Hbyp3) was designed to radially display nine hydrophobic bipyridine moieties from a triple helical scaffold. Self-assembly of such functionalized triple helices led to the formation of micrometer-scaled disks with a curved morphology, presumably mediated by aromatic interactions, with a height that is in the range of the length of the triple helical peptide. Higher order assembly of these curved disks into micrometer-sized hollow spheres was accomplished through metal-ligand interactions between bipyridine groups of the disks and metal ions such as Fe(II), Co(II), Zn(II) and Cu(II).

Metal-mediated tandem coassembly of collagen peptides into banded microstructures.

The ability to recapitulate the features of natural collagen at the micro- and nanoscale with novel biopolymers has the potential to lead to improved biomaterials. Herein we describe stimuli-responsive collagen-based peptides (IdaCol and HisCol) that together form higher order assemblies in the presence of added metal ions. SEM and TEM imaging of these assemblies revealed microscale petal-like and intertwined fiber morphologies, each with periodic banding on the nanometer scale.

Metal-triggered collagen peptide disk formation.

A collagen peptide was designed for metal-triggered, hierarchical assembly through a radial growth mechanism. To achieve radial assembly, H-(byp)(2) containing Pro-Hyp-Gly repeating sequences and two staggered bipyridine ligands within the peptide was synthesized. Triple helix formation resulted in the placement of six bipyridine ligands along the triple helix, and the addition of metal ions resulted in the formation of nanometer-sized collagen peptide disks.