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Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile

Dehsorkhi, A., Hamley, I. W. ORCID:, Seitsonen, J. and Ruokolainen, J. (2013) Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile. Langmuir, 29. pp. 6665-6672. ISSN 0743-7463

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To link to this item DOI: 10.1021/la401025r


The enzymatic cleavage of a peptide amphiphile (PA) is investigated. The self-assembly of the cleaved products is distinct from that of the PA substrate. The PA C16-KKFFVLK is cleaved by α-chymotrypsin at two sites leading to products C16-KKF with FVLK and C16-KKFF with VLK. The PA C16-KKFFVLK forms nanotubes and helical ribbons at room temperature. Both PAs C16-KKF and C16-KKFF corresponding to cleavage products instead self-assemble into 5-6 nm diameter spherical micelles, while peptides FVLK and VLK do not adopt well-defined aggregate structures. The secondary structures of the PAs and peptides are examined by FTIR and circular dichroism spectroscopy and X-ray diffraction. Only C16-KKFFVLK shows substantial β-sheet secondary structure, consistent with its self-assembly into extended aggregates, based on PA layers containing hydrogen-bonded peptide headgroups. This PA also exhibits a thermoreversible transition to twisted tapes on heating.

Item Type:Article
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:37320
Publisher:American Chemical Society


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