Conference Paper: Free-formed submicron-fabrication of protein matrix via multiphoton photochemical crosslinking

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TitleFree-formed submicron-fabrication of protein matrix via multiphoton photochemical crosslinking
AuthorsMa, J
Xu, J
Cheng, JP
Cheng, SH
Chan, BP
Issue Date2011
CitationThe 2011 Annual Meeting of the Asia Pacific Chapter of the Tissue Engineering and Regenerative Medicine International Society (TERMIS), Waterfront Conference Centre, Singapore, 3-5 August 2011. In Proceedings of the TERMIS Asia Pacific Meeting, 2011, p. 125 [How to Cite?]
AbstractPhotochemical crosslinking is effective in enhancing long-term stability of protein (e.g. collagen and fibronectin) structures without compromising the tissue compatibility. In this work, multiphoton-based photochemical crosslinking was used to fabricate protein structures with micron- and sub-micron-sized structures using bovine serum albumin (BSA) as the sample protein and rose Bengal (RB) as the photosensitizer. Our ultimate goal is to study how cells respond to patterned structures with sub-micron sized topological features. Arrays of BSA micro-pillars have been fabricated. Excellent 3D resolution in defining the shape of micro-pillar structures, either pyramidal or conical, was achieved by precisely controlling various scanning parameters and solution concentrations. The morphology of the protein structures fabricated was evaluated by multi-photon confocal microscopy and scanning electron microscopy (SEM).
DescriptionPoster Presentation
DC Field
Value
dc.contributor.authorMa, J
dc.contributor.authorXu, J
dc.contributor.authorCheng, JP
dc.contributor.authorCheng, SH
dc.contributor.authorChan, BP
dc.date.accessioned2011-09-23T06:11:03Z
dc.date.available2011-09-23T06:11:03Z
dc.date.issued2011
dc.description.abstractPhotochemical crosslinking is effective in enhancing long-term stability of protein (e.g. collagen and fibronectin) structures without compromising the tissue compatibility. In this work, multiphoton-based photochemical crosslinking was used to fabricate protein structures with micron- and sub-micron-sized structures using bovine serum albumin (BSA) as the sample protein and rose Bengal (RB) as the photosensitizer. Our ultimate goal is to study how cells respond to patterned structures with sub-micron sized topological features. Arrays of BSA micro-pillars have been fabricated. Excellent 3D resolution in defining the shape of micro-pillar structures, either pyramidal or conical, was achieved by precisely controlling various scanning parameters and solution concentrations. The morphology of the protein structures fabricated was evaluated by multi-photon confocal microscopy and scanning electron microscopy (SEM).
dc.descriptionPoster Presentation
dc.description.otherThe 2011 Annual Meeting of the Asia Pacific Chapter of the Tissue Engineering and Regenerative Medicine International Society (TERMIS), Waterfront Conference Centre, Singapore, 3-5 August 2011. In Proceedings of the TERMIS Asia Pacific Meeting, 2011, p. 125
dc.identifier.citationThe 2011 Annual Meeting of the Asia Pacific Chapter of the Tissue Engineering and Regenerative Medicine International Society (TERMIS), Waterfront Conference Centre, Singapore, 3-5 August 2011. In Proceedings of the TERMIS Asia Pacific Meeting, 2011, p. 125 [How to Cite?]
dc.identifier.epage125
dc.identifier.hkuros196506
dc.identifier.spage125
dc.identifier.urihttp://hdl.handle.net/10722/140406
dc.languageeng
dc.relation.ispartofProceedings of the TERMIS Asia Pacific Meeting
dc.titleFree-formed submicron-fabrication of protein matrix via multiphoton photochemical crosslinking
dc.typeConference_Paper