The binding pockets of extant enzymes feature precise positioning of amino acid residues that facilitate multiple complex transformations exploiting covalent and non-covalent interactions. Reversible covalent anchoring is extensively used as an efficient tool by Nature for activating modern enzymes such as esterases and dehydratases and also for proteins like opsins for the complex process of visual phototransduction. Here, we developed paracrystalline amyloid surfaces through the self-propagation of short peptides which offer binding pockets, exposed with arrays of imidazoles and lysines. These homogeneous amyloid nanotubes exploit Schiff imine formation via the exposed lysines to efficiently hydrolyze both activated and inactivated esters by the imidazole residues. Further, we report the catalytic potential of surface exposed histidine of cross-β amyloid nanotubes showing facile hydrolase -peroxidase cascade reactions in presence of hemin, the prosthetic group of extant peroxidases. Further, evidence suggested that these self-assembled nanotubes foreshadow the process of intermediate channeling, a feature seen in the case of advanced enzymes.

Cross-β Amyloid Nanotubes for Covalent Catalysis to Hydrolase–Peroxidase Cascade Reaction.

In order to view the entire gallery of posters, videos, and other materials, please click "Submissions" below. 

To find the Q&A for each poster category, please click "Sessions" below. 

To ask a question, simply click on the session of interest. You will see a list of video presentations to the right. Below each video area, you'll see a section entitled 'Q&A for this presentation'. Here you can post questions to the presenters. They will be notified, and you'll also be notified when they reply to your question. You can expect that notification by email, and you'll find the author's response here.

27th CRSI National Symposium in Chemistry

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.