Molecular design principles of Lysine-DOPA wet adhesion.

The mussel byssus has long been a source of inspiration for the adhesion community. Recently, adhesive synergy between flanking lysine (Lys, K) and 3,4-Dihydroxyphenylalanine (DOPA, Y) residues in the mussel foot proteins (Mfps) has been highlighted. However, the complex topological relationship of DOPA and Lys as well as the interfacial adhesive roles of other amino acids have been understudied.

Nanoparticle-based highly sensitive MRI contrast agents with enhanced relaxivity in reductive milieu.

Current magnetic resonance imaging (MRI) contrast agents often produce insufficient contrast for diagnosis of early disease stages, and do not sense their biochemical environments. Herein, we report a highly sensitive nanoparticle-based MRI probe with r1 relaxivity up to 51.7 ± 1.

Stimuli-Responsive Codelivery of Oligonucleotides and Drugs by Self-Assembled Peptide Nanoparticles.

Ever more emerging combined treatments exploiting synergistic effects of drug combinations demand smart, responsive codelivery carriers to reveal their full potential. In this study, a multifunctional stimuli-responsive amphiphilic peptide was designed and synthesized to self-assemble into nanoparticles capable of co-bearing and -releasing hydrophobic drugs and antisense oligonucleotides for combined therapies. The rational design was based on a hydrophobic l-tryptophan-d-leucine repeating unit derived from a truncated sequence of gramicidin A (gT), to entrap hydrophobic cargo, which is combined with a hydrophilic moiety of histidines to provide electrostatic affinity to nucleotides.

Self-assembled peptide beads used as a template for ordered gold nanoparticle superstructures.

Using peptide-based materials to tailor self-assembled, nano-scaled hybrid materials with potentially high biocompatibility/biodegradability is gaining importance in developing a broad range of new applications, in areas such as diagnostics and medicine. Here, we investigated how the self-assembly ability of amphiphilic peptides can be used to create organized inorganic materials, i.e.

Hemoglobin and red blood cells catalyze atom transfer radical polymerization.

Hemoglobin (Hb) is a promiscuous protein that not only transports oxygen, but also catalyzes several biotransformations. A novel in vitro catalytic activity of Hb is described. Bovine Hb and human erythrocytes were found to display ATRPase activity, i.

Self-assembled structures from amphiphilic peptides.

Nanotechnology and its applications are strongly influenced by structures self-assembled from a variety of different materials. This review covers nanostructures, including micelles, rod-like micelles, fibers and peptide beads, self-assembled from de novo designed amphiphilic peptides. The latter are promising candidates for the development of nanoscale carrier systems because they are completely composed of amino acids.

Horseradish peroxidase as a catalyst for atom transfer radical polymerization.

The hemoprotein horseradish peroxidase (HRP) catalyzes the polymerization of N-isopropylacrylamide with an alkyl bromide initiator under conditions of activators regenerated by electron transfer atom transfer radical polymerization (ARGET ATRP) in the absence of any peroxide. This is a novel activity of HRP, which we propose to name ATRPase activity. Bromine-terminated polymers with polydispersity indices (PDIs) as low as 1.