Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.biomaterials.2008.02.009
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dc.titleElectro-spinning of pure collagen nano-fibres - Just an expensive way to make gelatin?
dc.contributor.authorZeugolis, D.I.
dc.contributor.authorKhew, S.T.
dc.contributor.authorYew, E.S.Y.
dc.contributor.authorEkaputra, A.K.
dc.contributor.authorTong, Y.W.
dc.contributor.authorYung, L.-Y.L.
dc.contributor.authorHutmacher, D.W.
dc.contributor.authorSheppard, C.
dc.contributor.authorRaghunath, M.
dc.date.accessioned2014-06-17T07:39:51Z
dc.date.available2014-06-17T07:39:51Z
dc.date.issued2008-05
dc.identifier.citationZeugolis, D.I., Khew, S.T., Yew, E.S.Y., Ekaputra, A.K., Tong, Y.W., Yung, L.-Y.L., Hutmacher, D.W., Sheppard, C., Raghunath, M. (2008-05). Electro-spinning of pure collagen nano-fibres - Just an expensive way to make gelatin?. Biomaterials 29 (15) : 2293-2305. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biomaterials.2008.02.009
dc.identifier.issn01429612
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/63815
dc.description.abstractScaffolds manufactured from biological materials promise better clinical functionality, providing that characteristic features are preserved. Collagen, a prominent biopolymer, is used extensively for tissue engineering applications, because its signature biological and physico-chemical properties are retained in in vitro preparations. We show here for the first time that the very properties that have established collagen as the leading natural biomaterial are lost when it is electro-spun into nano-fibres out of fluoroalcohols such as 1,1,1,3,3,3-hexafluoro-2-propanol or 2,2,2-trifluoroethanol. We further identify the use of fluoroalcohols as the major culprit in the process. The resultant nano-scaffolds lack the unique ultra-structural axial periodicity that confirms quarter-staggered supramolecular assemblies and the capacity to generate second harmonic signals, representing the typical crystalline triple-helical structure. They were also characterised by low denaturation temperatures, similar to those obtained from gelatin preparations (p > 0.05). Likewise, circular dichroism spectra revealed extensive denaturation of the electro-spun collagen. Using pepsin digestion in combination with quantitative SDS-PAGE, we corroborate great losses of up to 99% of triple-helical collagen. In conclusion, electro-spinning of collagen out of fluoroalcohols effectively denatures this biopolymer, and thus appears to defeat its purpose, namely to create biomimetic scaffolds emulating the collagen structure and function of the extracellular matrix. © 2008 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.biomaterials.2008.02.009
dc.sourceScopus
dc.subjectCircular dichroism
dc.subjectCollagen denaturation
dc.subjectDenaturation temperature
dc.subjectGelatin
dc.subjectSecond harmonic generation
dc.subjectTransmission electron microscopy
dc.typeArticle
dc.contributor.departmentBIOENGINEERING
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1016/j.biomaterials.2008.02.009
dc.description.sourcetitleBiomaterials
dc.description.volume29
dc.description.issue15
dc.description.page2293-2305
dc.description.codenBIMAD
dc.identifier.isiut000255088700001
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