Nanoparticle Formation of Ovalbumin with Cationic Oligopeptides

Anomalous Conformational Instability and Hydrogel Formation of a Cationic Class of Self-Assembling Oligopeptides

A detailed understanding of themechanistic principles which govern peptide and protein selfassembly is of considerable biomedical and biotechnological importance. Owing to the diversity of peptide and protein sequences which have been shown to aggregate into ordered structures, the ability to self-assemble is now recognized as an inherent feature of the polypeptide backbone. It is therefore of ...

α-helix formation rate of oligopeptides at subzero temperatures

In 1999, Clarke et al. ((1999) Proc. Natl. Acad. Sci. USA 96, 7232-7237) reported that the nucleation rate of α-helix of oligopeptide AK16 is as slow as 60 ms. In the present study, we measured the nucleation rate of oligopeptide, C17 (DLTDDIMCVKKILDKVG, corresponding to α-helical region of 84th to 100th amino acids of bovine α-lactalbumin) using the same method as Clarke et al. We found only i...

Formation of oligopeptides in high yield under simple programmable conditions

Many high-yielding reactions for forming peptide bonds have been developed but these are complex, requiring activated amino-acid precursors and heterogeneous supports. Herein we demonstrate the programmable one-pot dehydration-hydration condensation of amino acids forming oligopeptide chains in around 50% yield. A digital recursive reactor system was developed to investigate this process, perfo...

Effects of Cationic Proteins on Gold Nanoparticle/Aptamer Assays

Gold nanoparticles (AuNPs) and aptamers are compelling building blocks for analytical assays with desired attributes of selectivity and sensitivity and may theoretically form the basis of instrument-free color-changing assays for any target against which a DNA aptamer has been selected. However, assays for proteins based on these components may be subject to significant interferences from the i...

Cellulose Functionalysed with Grafted Oligopeptides