Nanostructure of electrospun collagen: Do electrospun collagen fibers form native structures?

Autor: Johan Potgieter, Kathleen Hofman, Adrian Hawley, Danielle E. Martin, Mathew H. Cumming, Katie H. Sizeland, Stephen T. Mudie, Ian C. Hallett, Timothy M. Ryan, Richard G. Haverkamp, Nigel Kirby
Rok vydání: 2018
Předmět:
Zdroj: Materialia. 3:90-96
ISSN: 2589-1529
Popis: Collagen extracts can be electrospun to form fibers. The nanoscale structure of these fibers is not known but is expected to affect the biocompatibility of the spun materials. Collagen extracts from Macruronus novaezelandiae (hoki) skin were electrospun to form a fibrous material. The structure of the electrospun collagen fibers was analyzed and compared with the structure of native collagen, gelatin, and electrospun gelatin. Attenuated Total Reflectance Fourier Transform Infrared spectroscopy (ATR-FTIR) and SDS-PAGE were used to characterize the basic molecular structure of the biomaterials and synchrotron-based small-angle X-ray scattering (SAXS) and Transmission electron microscope (TEM) were used to investigate the fibril nanoscale structure (molecular arrangement). ATR-FTIR and SDS-PAGE revealed characteristic patterns of intact alpha chains in the electrospun collagen and hydrolyzed fragments in electrospun gelatin, as expected. TEM revealed fibers in both the native collagen material and the electrospun samples. However, SAXS patterns showed axial periodicity was not present in the electrospun fibers. This is indicative of the spinning process forming fibers that lack internal fibril structure, in contrast to the hierarchical structure of native collagen. The architecture of collagen affects its function. By characterizing the molecular and fibril structure of electrospun collagen and comparing it with native collagen fibrils, we may inform functional studies of collagen, including its configuration for cell attachment and recognition.
Databáze: OpenAIRE
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