4.6 Article

Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure

期刊

SOFT MATTER
卷 8, 期 20, 页码 5434-5438

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ROYAL SOC CHEMISTRY
DOI: 10.1039/c2sm25546d

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资金

  1. EPSRC [EP/G030952/1, EP/G026203/1]
  2. Royal Society
  3. EPSRC [EP/F048114/1, EP/G030952/1, EP/G026203/1] Funding Source: UKRI
  4. Engineering and Physical Sciences Research Council [EP/G030952/1, EP/G026203/1, EP/F048114/1] Funding Source: researchfish

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The self-assembly in aqueous solution of PEG-peptide conjugates comprising a model amyloid peptide sequence FFKLVFF that contains the Ab(16-20) KLVFF motif is investigated. X-ray diffraction reveals different packing motifs dependent on PEG chain length. This is correlated to remarkable differences in self-assembled nanostructures. The control of strand registry points to a subtle interplay between aromatic stacking, electrostatic and amphiphilic interactions.

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