File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Effects of photochemical crosslinking on the microstructure of collagen and a feasibility study on controlled protein release

TitleEffects of photochemical crosslinking on the microstructure of collagen and a feasibility study on controlled protein release
Authors
KeywordsCollagen
Microstructure
Photochemical crosslinking
Protein release
Issue Date2008
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/actabiomat
Citation
Acta Biomaterialia, 2008, v. 4 n. 6, p. 1627-1636 How to Cite?
AbstractPhotochemical crosslinking is an emerging technique able to modify the physicochemical properties of collagen. However, whether this technique can be used to modify collagen-based structures for drug delivery has not been studied. This study demonstrated that the microporous structure of photochemically crosslinked collagen was affected by rose Bengal and laser energy level. Using the optimized process parameters, the authors fabricated photochemically crosslinked collagen structures encapsulated with sample proteins and demonstrated that photochemical crosslinking reduced the initial burst effect and protein release without compromising the protein bioactivity. The fiber meshwork in collagen structures was also characterized, and it was found that photochemical crosslinking did not significantly alter the mesh size. This study reports the effects of photochemical crosslinking on the microstructure of collagen structures and suggests the feasibility of using photochemically crosslinked collagen structures for controlled protein release. © 2008 Acta Materialia Inc.
Persistent Identifierhttp://hdl.handle.net/10722/67946
ISSN
2015 Impact Factor: 6.008
2015 SCImago Journal Rankings: 2.020
ISI Accession Number ID
Funding AgencyGrant Number
Research Grant Council (RGC)
Innovation and Technology Commission (ITC) of the Hong Kong Government
University Research Committee
University of Hong Kong10205248
10206115
Funding Information:

This work was supported by Research Grant Council (RGC), Innovation and Technology Commission (ITC) of the Hong Kong Government, and University Research Committee, the University of Hong Kong (Nos. 10205248 and 10206115). The authors thank Ms. H.L. Wong and Mr. K.L. Au-Yeung for assistance with the pore size measurements.

References

 

DC FieldValueLanguage
dc.contributor.authorChan, BPen_HK
dc.contributor.authorChan, OCMen_HK
dc.contributor.authorSo, KFen_HK
dc.date.accessioned2010-09-06T05:59:42Z-
dc.date.available2010-09-06T05:59:42Z-
dc.date.issued2008en_HK
dc.identifier.citationActa Biomaterialia, 2008, v. 4 n. 6, p. 1627-1636en_HK
dc.identifier.issn1742-7061en_HK
dc.identifier.urihttp://hdl.handle.net/10722/67946-
dc.description.abstractPhotochemical crosslinking is an emerging technique able to modify the physicochemical properties of collagen. However, whether this technique can be used to modify collagen-based structures for drug delivery has not been studied. This study demonstrated that the microporous structure of photochemically crosslinked collagen was affected by rose Bengal and laser energy level. Using the optimized process parameters, the authors fabricated photochemically crosslinked collagen structures encapsulated with sample proteins and demonstrated that photochemical crosslinking reduced the initial burst effect and protein release without compromising the protein bioactivity. The fiber meshwork in collagen structures was also characterized, and it was found that photochemical crosslinking did not significantly alter the mesh size. This study reports the effects of photochemical crosslinking on the microstructure of collagen structures and suggests the feasibility of using photochemically crosslinked collagen structures for controlled protein release. © 2008 Acta Materialia Inc.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/actabiomaten_HK
dc.relation.ispartofActa Biomaterialiaen_HK
dc.rightsActa Biomaterialia. Copyright © Elsevier BV.en_HK
dc.subjectCollagenen_HK
dc.subjectMicrostructureen_HK
dc.subjectPhotochemical crosslinkingen_HK
dc.subjectProtein releaseen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshCattleen_HK
dc.subject.meshCollagen - chemistryen_HK
dc.subject.meshCross-Linking Reagents - pharmacologyen_HK
dc.subject.meshDrug Carriers - chemistryen_HK
dc.subject.meshDrug Delivery Systemsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMicroscopy, Electron, Scanningen_HK
dc.subject.meshNerve Growth Factoren_HK
dc.subject.meshPhotochemistry - methodsen_HK
dc.subject.meshPhotosensitizing Agents - pharmacologyen_HK
dc.subject.meshProteins - chemistryen_HK
dc.subject.meshRose Bengal - chemistryen_HK
dc.subject.meshSerum Albumin, Bovine - chemistryen_HK
dc.subject.meshSolubilityen_HK
dc.titleEffects of photochemical crosslinking on the microstructure of collagen and a feasibility study on controlled protein releaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1742-7061&volume=4&spage=1627&epage=1636&date=2008&atitle=Effects+of+photochemical+crosslinking+on+the+microstructure+of+collagen+and+a+feasibility+study+on+controlled+protein+releaseen_HK
dc.identifier.emailChan, BP:bpchan@hkucc.hku.hken_HK
dc.identifier.emailSo, KF:hrmaskf@hkucc.hku.hken_HK
dc.identifier.authorityChan, BP=rp00087en_HK
dc.identifier.authoritySo, KF=rp00329en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.actbio.2008.06.007en_HK
dc.identifier.pmid18640085-
dc.identifier.scopuseid_2-s2.0-53649108017en_HK
dc.identifier.hkuros147710en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-53649108017&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume4en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1627en_HK
dc.identifier.epage1636en_HK
dc.identifier.isiWOS:000261253400006-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridChan, BP=7201530390en_HK
dc.identifier.scopusauthoridChan, OCM=23049435400en_HK
dc.identifier.scopusauthoridSo, KF=34668391300en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats