Insights into the Hierarchical Assembly of a Chemically Diverse Peptide Hydrogel Derived from Human Semenogelin I.

A peptide corresponding to a 13-residue segment of the human protein semenogelin I has been shown to generate a hydrogel consisting of amyloid-like fibrils. The relative chemical diversity (compared to synthetic sequences) with 11 distinct amino acids makes this peptide (P0) an ideal candidate for investigating the role of individual residues in gelation. Herein, the terminal residues have been sequentially removed to furnish a series of truncated peptides, P1-P10, ranging from 12 to 3 residues in length.

On the Mechanism of Self-Assembly by a Hydrogel-Forming Peptide.

Self-assembling peptide-based hydrogels are a class of tunable soft materials that have been shown to be highly useful for a number of biomedical applications. The dynamic formation of the supramolecular fibrils that compose these materials has heretofore remained poorly characterized. A better understanding of this process would provide important insights into the behavior of these systems and could aid in the rational design of new peptide hydrogels.

Elevated Intra-Articular Cobalt and Chromium Levels in Mechanically Assisted Crevice Corrosion in Metal-on-Polyethylene Total Hip Arthroplasty.

Background: Failed total hip arthroplasty (THA) caused by mechanically assisted crevice corrosion (MACC) has serious consequences such as adverse local tissue reaction (ALTR). Serum cobalt (Co) and chromium (Cr) ion levels have been used to diagnose taper corrosion, but have not been shown to be an accurate measure of the severity of MACC or associated ALTRs. Additionally, elevated serum ions are not specific in patients with multiple artificial joints.