Congratulations to PhD student Raffaella Parlato, as well as our collaborators from the group of Marleen Kamperman, with the publication of a new collaborative paper in the journal Communications Chemistry. Raffaella used solid-state NMR to study the structure and dynamics of (labeled) polypeptides within the hybrid polymer-peptide materials prepared by the Kamperman group. The employed peptides are poly-alanine peptides inspired by the structural motifs found in proteins in spider silk. Spider silk proteins use polyalanine segments to form stable higher order structures that enable the remarkable materials properties of silk. Here, these peptides were used to change the materials properties of a coacervate, as shown by various rheological analyses.
By isotopically labeling the peptides (with non-radioactive 13C and 15N) it becomes possible to see their structure and dynamics by ssNMR, even in the complex samples with non-peptide components. Indeed, 1D and 2D NMR measurements revealed the different secondary structures adopted by the peptides, their interactions and dynamics. This provides insights into their structural role in the soft material matrix.
For more information and details, see the paper online at the journal:
Amirsadeghi, A.; Parlato, R.; Kenbeek, A.; Gaspar, A. R.; Oggioni, M.; Lasorsa, A.; Mukherjee, A.; Jaber, M.; Włodarczyk-Biegun, M. K.; Van Der Wel, P. C. A.; Kamperman, M.; Monreal Santiago, G. Crosslinking, Salt-Induced Aging, and Secondary Structure Formation in Peptide-Containing Coacervates Inspired by Spider Silk. Commun Chem 2025, 8 (1), 264. https://doi.org/10.1038/s42004-025-01634-8.
