Please use this identifier to cite or link to this item:
|Title:||Enzymatically crosslinked collagen-mimetic dendrimers that promote integrin-targeted cell adhesion||Authors:||Khew, S.T.
|Issue Date:||Jul-2008||Citation:||Khew, S.T., Yang, Q.J., Tong, Y.W. (2008-07). Enzymatically crosslinked collagen-mimetic dendrimers that promote integrin-targeted cell adhesion. Biomaterials 29 (20) : 3034-3045. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biomaterials.2008.03.023||Abstract:||Collagen is made up of a diverse family of the extracellular matrices, most of which are generally found crosslinked in vivo. To more closely mimic the biological function of collagen, this work focuses on establishing a molecular strategy to engineer a functional biomimetic collagen that exhibits stable collagen-like triple-helical conformation with cell-binding activity, in addition to an enzyme-mediated crosslinking by tissue transglutaminase (tTGase). A novel sequence spanning residues 2800-2807 of human fibrillin-1 (EDGFFKI) was first identified as an amine donor substrate for tTGase, using a previously characterized APQQEA derived from human osteonectin as an amine acceptor probe. Subsequently, collagen-mimetic peptides (CMPs) supplemented with a cell-binding sequence (GFOGER) and the identified EDGFFKI and APQQEA substrate sequences were conjugated onto a generation 2 poly(amidoamine) dendrimer, resulting in a crosslinkable collagen-mimetic dendrimer, denoted as CMD-K and CMD-Q, respectively. Both CMD-K and CMD-Q exhibited enhanced triple-helical stability and supported cell adhesion in an integrin-specific manner. Finally, tTGase-mediated crosslinking between CMD-K and CMD-Q resulted in a supramolecular structure that exhibited stable collagen-like triple-helical conformation and improved cellular recognition. The results show that the triple-helical structure is important in preserving the GFOGER cell-binding site while the tTGase-mediated protein crosslinking may also be crucial for the recognition by cell surface integrin receptors. © 2008 Elsevier Ltd. All rights reserved.||Source Title:||Biomaterials||URI:||http://scholarbank.nus.edu.sg/handle/10635/63858||ISSN:||01429612||DOI:||10.1016/j.biomaterials.2008.03.023|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Oct 18, 2021
WEB OF SCIENCETM
checked on Oct 18, 2021
checked on Oct 14, 2021
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.