Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres

TY - JOUR

T1 - Super-resolution microscopy reveals structural diversity in molecular exchange among peptide amphiphile nanofibres

AU - da Silva, Ricardo M. P.

AU - van der Zwaag, Daan

AU - Albertazzi, Lorenzo

AU - Lee, Sungsoo S.

AU - Meijer, E. W.

AU - Stupp, Samuel I.

PY - 2016/5

Y1 - 2016/5

N2 - 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.

AB - 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.

KW - Chemical biology

KW - Chemical sciences

KW - Nanotechnology

KW - Physical Chemistry

U2 - 10.1038/ncomms11561

DO - 10.1038/ncomms11561

M3 - Article

SN - 2041-1723

VL - 7

SP - 1

EP - 10

JO - Nature Communications

JF - Nature Communications

M1 - 11561

ER -