Researchers of the laboratories of FMS prof. Bert Meijer (ICMS, TU/e) and prof. Samuel Stupp (Northwestern University, USA) have published their research in Nature Communications in an article entitled: Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres.
The dynamic behaviour of supramolecular systems is an important dimension of their potential functions. Here, we report on the use of stochastic optical reconstruction microscopy to study the molecular exchange of peptide amphiphile nanofibres, supramolecular systems known to have important biomedical functions. Solutions of nanofibres labelled with different dyes (Cy3 and Cy5) were mixed, and the distribution of dyes inserting into initially single-colour nanofibres was quantified using correlative image analysis. Our observations are consistent with an exchange mechanism involving monomers or small clusters of molecules inserting randomly into a fibre. Different exchange rates are observed within the same fibre, suggesting that local cohesive structures exist on the basis of β-sheet discontinuous domains. The results reported here show that peptide amphiphile supramolecular systems can be dynamic and that their intermolecular interactions affect exchange patterns. This information can be used to generate useful aggregate morphologies for improved biomedical function.
Ricardo M.P. da Silva, Daan van der Zwaag, Lorenzo Albertazzi, Sungsoo S. Lee, E.W. Meijer & Samuel I. Stupp. Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres, Nature Communications (2016), doi: 10.1038/ncomms11561