Supramolecular Nanostructure Formation of Coassembled Amyloid Inspired Peptides


Cinar G., ORUJALIPOOR I., Su C., Jeng U., İDE S. , Guler M. O.

LANGMUIR, cilt.32, ss.6506-6514, 2016 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 32 Konu: 25
  • Basım Tarihi: 2016
  • Doi Numarası: 10.1021/acs.langmuir.6b00704
  • Dergi Adı: LANGMUIR
  • Sayfa Sayıları: ss.6506-6514

Özet

Characterization of amyloid-like aggregates through converging approaches can yield deeper understanding of their complex self-assembly mechanisms and the nature of their strong mechanical stability, which may in turn contribute to the design of novel supramolecular peptide nano structures as functional materials. In this study, we investigated the coassembly kinetics of oppositely charged short amyloidinspired peptides (AlPs) into supramolecular nanostructures by using confocal fluorescence imaging of thioflavin T binding, turbidity assay and in situ small-angle X-ray scattering (SAXS) analysis. We showed that coassembly kinetics of the AIP nanostructures were consistent with nucleation-dependent amyloid-like aggregation, and aggregation behavior of the AlPs was affected by the initial monomer concentration and sonication. Moreover, SAXS analysis was performed to gain structural information on the size, shape, electron density, and internal organization of the coassembled AIP nanostructures. The scattering data of the coassembled AIP nanostructures were best fitted into to a combination of polydisperse core shell cylinder (PCSC) and decoupling flexible cylinder (FCPR) models, and the structural parameters were estimated based on the fitting results of the scattering data. The stability of the coassembled AIP nanostructures in both fiber organization and bulk viscoelastic properties was also revealed via temperature-dependent SAXS analysis and oscillatory rheology measurements, respectively.