Self-assembling short peptides have attracted great interest as enzyme mimics, especially if the catalytic activity resides solely in the supramolecular structure so that it can be switched on/off as needed by controlling assembly/disassembly. Among the various enzyme classes, hydrolases find wide application in biomaterials, and their mimetics often contain His residues, in addition to either divalent cations or other amino acids to mimic the catalytic site. This work reports two self-assembling tetrapeptides based on the Ser-His motif for catalysis and the Phe-Phe motif to drive amyloid structure formation.
View Article and Find Full Text PDFBioactive hydrogels based on the self-assembly of tripeptides have attracted great interest in recent years. In particular, the search is active for sequences that are able to mimic enzymes when they are self-organized in a nanostructured hydrogel, so as to provide a catalytic (bio)material whose activity can be switched on/off with assembly/disassembly. Within the diverse enzymes that have been targeted for mimicry, hydrolases find wide application in biomaterials, ranging from their use to convert prodrugs into active compounds to their ability to work in reverse and catalyze a plethora of reactions.
View Article and Find Full Text PDFClinical and radiological studies of the fractured teeth of patients between seven and eleven years old were conducted to assess the use of permanent and immediate (emergency) techniques for reconstructing anterior permanent teeth with immature apices. The general hypothesis states that, given the physical and biocompatible properties of the materials used in the immediate (emergency) technique, there are no significant differences between the two techniques as far as pulp vitality and apical growth are concerned. A sample of fifty-six patients was selected.
View Article and Find Full Text PDF