Date: 03-10-2025
Time: 1:00-2:00 pm
Venue: an online Zoom seminar (register to join)
Dr Andy Nguyen
Assistant Professor at the University of Illinois Chicago
鈥淩eplication and mimicry of metalloenzyme active sites in peptide frameworks鈥�
Metalloenzymes efficiently catalyze some of the most challenging chemical transformations, many of which are critical to a sustainable society. Learning how to construct similar synthetic mimics by a bottom-up approach would both enhance our understanding of metalloenzymes and allow for the design of highly active artificial catalysts. Model compounds have long focused on the metal center(s), but it is now clear that the contribution of the protein scaffold needs to be addressed. However, the synthesis and structural characterization of elaborate protein-like ligands are major barriers towards the rational synthetic mimicry of the protein scaffold. To address these gaps, our laboratory has developed an approach to rapidly generate molecularly defined, protein-like platforms via the self-assembly of peptides. We design small, chemically synthesized peptides that assemble into porous crystalline materials (also called 鈥渇rameworks鈥�) that can bind metals and have multiple variable positions for rapid engineering of the secondary sphere. Furthermore, nearly all peptide frameworks form single crystals suitable for X-ray diffraction, allowing determination of detailed structural-functional relationships. The modularity and ease of peptide synthesis enables a practical synthetic approach to test how minimalist protein-like environments may elicit remarkable inorganic reactivity.
Prof Silvia Marchesan
Associate Professor at the University of Trieste
鈥淐hirality effects in peptide self-assembly鈥�
Our group investigates the effects of variations in amino acid stereoconfiguration for the self-assembly of short heterochiral peptides. Applications are varied and span from enzyme mimicry, to amyloid fibrillation inhibition, to biomaterials for cell culture and tissue regeneration. We are particularly interested in studying self-assembling processes all the way from the nanoscale to the macroscale. Most recent works have focused on supramolecular peptide nanotubes that could find various applications for the storage and delivery of a variety of guests.
Time: 1:00-2:00 pm
Venue: an online Zoom seminar (register to join)
Dr Andy Nguyen
Assistant Professor at the University of Illinois Chicago
鈥淩eplication and mimicry of metalloenzyme active sites in peptide frameworks鈥�
Metalloenzymes efficiently catalyze some of the most challenging chemical transformations, many of which are critical to a sustainable society. Learning how to construct similar synthetic mimics by a bottom-up approach would both enhance our understanding of metalloenzymes and allow for the design of highly active artificial catalysts. Model compounds have long focused on the metal center(s), but it is now clear that the contribution of the protein scaffold needs to be addressed. However, the synthesis and structural characterization of elaborate protein-like ligands are major barriers towards the rational synthetic mimicry of the protein scaffold. To address these gaps, our laboratory has developed an approach to rapidly generate molecularly defined, protein-like platforms via the self-assembly of peptides. We design small, chemically synthesized peptides that assemble into porous crystalline materials (also called 鈥渇rameworks鈥�) that can bind metals and have multiple variable positions for rapid engineering of the secondary sphere. Furthermore, nearly all peptide frameworks form single crystals suitable for X-ray diffraction, allowing determination of detailed structural-functional relationships. The modularity and ease of peptide synthesis enables a practical synthetic approach to test how minimalist protein-like environments may elicit remarkable inorganic reactivity.
Prof Silvia Marchesan
Associate Professor at the University of Trieste
鈥淐hirality effects in peptide self-assembly鈥�
Our group investigates the effects of variations in amino acid stereoconfiguration for the self-assembly of short heterochiral peptides. Applications are varied and span from enzyme mimicry, to amyloid fibrillation inhibition, to biomaterials for cell culture and tissue regeneration. We are particularly interested in studying self-assembling processes all the way from the nanoscale to the macroscale. Most recent works have focused on supramolecular peptide nanotubes that could find various applications for the storage and delivery of a variety of guests.
