Heterochirality in peptides self-assembly: the situation beyond the mirror

Place: Hinarejos room (ground floor) and online

Zoom link: https://nanoscience-imdea.zoom.us/j/99236405128

Abstract: 

Inspired by nature, scientists use bottom-up approaches where synthetic building blocks self-organize into specific, supramolecular architectures with desired properties. In this context, short peptides are attractive self-assembling motifs that mimics naturally occurring proteins while their simplicity favor the use of chemical tools to better explore and control functionality. Peptides stand out for their chemical diversity, low impact on the environment, and ability to convey biological messages in sequences as short as three amino acids. The 20 natural amino acids provide a diverse “toolbox” in supramolecular chemistry that allows organization at the macroscale level that can be tailored and fine-tuned from their monomeric chemical structure (e.g., synthesis). The combination of L- and D-amino acids in the same peptide sequence has been used as a novel approach to achieve self-assembling peptide hydrogels. A combination of experimental and theoretical techniques helped us to decipher the rules that favor gelation only in heterochiral sequences. Moreover, the influence of peptide sequence or their combination with other supramolecular entities have been studied, leading to supramolecular functional materials that have been exploited in applications as biocatalysis, amyloid aggregation inhibition or chemical separation, among others.