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Lookup NU author(s): Merlin Walter, Professor Che ConnonORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
The self-assembly and bioactivity of a peptide amphiphile (PA) incorporating a 13-residue sequence derived from the last 13 amino acids of the C-terminus of lumican, many types of tissue and is involved in collagen fibril the PA was determined through pyrene fluorescence measure-organization. A critical aggregation concentration (C-16) for C-16-YEALRVANEVTLN, attached to a hexadecyl (C-16) lipid in chain have been examined. Lumican is a proteoglycan found meats. The structure of the aggregates was imaged using electron microscopy, and twisted and curved nanotapes were observed. In situ small-angle X-ray scattering and fiber X-ray diffraction reveal that these tapes contain interdigitated bilayers of the PA molecules. FTIR and circular dichroism spectroscopy and fiber X-ray diffraction indicate that the lumican sequence in the PA adopts a beta-sheet secondary structure. Cell assays using human dermal fibroblasts show that below the cac the PA displays good biocompatibility and also stimulates collagen production over a period of 3 weeks, exceeding a 2-fold enhancement for several concentrations. Thus, this PA has promise in future biological applications, in particular, in tissue engineering.
Author(s): Hamley IW, Dehsorkhi A, Castelletto V, Walter MNM, Connon CJ, Reza M, Ruokolainen J
Publication type: Article
Publication status: Published
Journal: Langmuir
Year: 2015
Volume: 31
Issue: 15
Pages: 4490-4495
Online publication date: 02/04/2015
Date deposited: 09/06/2015
ISSN (print): 0743-7463
ISSN (electronic): 1520-5827
Publisher: American Chemical Society
URL: http://dx.doi.org/10.1021/acs.langmuir.5b00057
DOI: 10.1021/acs.langmuir.5b00057
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