eprintid: 76748 rev_number: 13 eprint_status: archive userid: 16805 dir: disk0/00/07/67/48 datestamp: 2013-03-19 12:02:51 lastmod: 2025-05-01 22:40:07 status_changed: 2013-03-19 12:02:51 type: article metadata_visibility: show creators_name: Coelho, N.M. creators_name: Gonzalez-Garcia, C. creators_name: Salmerón-Sánchez, M. creators_name: Altankov, G. creators_orcid: 0000-0002-8112-2100 title: Arrangement of type IV collagen and laminin on substrates with controlled density of –OH groups ispublished: pub divisions: 30303000 abstract: Collagen IV (Col IV) and laminin (Lam) are the main structural components of the basement membrane where they form two overlapping polymeric networks. We studied the adsorption pattern of these proteins on five model surfaces with tailored density of –OH groups obtained by copolymerization of different ratios ethyl acrylate (EA) and hydroxyl EA (HEA): <sup>X</sup>OH=<sup>0</sup>, <sup>X</sup>OH=<sup>0.3</sup>, <sup>X</sup>OH=<sup>0.5</sup>, <sup>X</sup>OH=<sup>0.7</sup>, and <sup>X</sup>OH=<sup>1</sup> (where X refers the ratio of HEA). Atomic force microscopy revealed substratum-specific adsorption patterns of Col IV and Lam, ranging from single molecules deposition on more hydrophilic substrata to the formation of complex networks on hydrophobic ones. Human umbilical endothelial cells were used to study the biological performance of adsorbed proteins, following the overall cell morphology, the quantities for cell adhesion and spreading, and the development of focal adhesion complexes and actin cytoskeleton. Surprisingly, two optima in the cellular interaction were observed—one on the most hydrophilic <sup>X</sup>OH=<sup>1</sup>and other on the relatively hydrophobic <sup>X</sup>OH=<sup>0.3</sup> substrate–valid for both Col IV and Lam. When the proteins were adsorbed consecutively, a hydrophobic shift to <sup>X</sup>OH=<sup>0</sup> substratum was obtained. Collectively, these data suggest that varying with the density of –OH groups one can tailor the conformation and the functional activity of adsorbed basement membrane proteins. date: 2011-08-25 date_type: published id_number: 10.1089/ten.tea.2010.0713 uniqueid: glaseprints:2011-76748 published_online: 2011-06-20 issn_online: 1937-335X scopus_impact: 3 scopus_cluster: 2-s2.0-80053151272 scopus_datestamp: 2013-10-26 09:26:56 wos_impact: 2 wos_cluster: WOS:000294303700012 wos_datestamp: 2013-05-21 22:53:58 full_text_status: none publication: Tissue Engineering Part A volume: 17 number: 17-18 pagerange: 2245-2257 refereed: TRUE issn: 1937-3341 hoa_compliant: 305 hoa_date_pub: 2011-06-20 hoa_exclude: FALSE hoa_gold: FALSE citation: Coelho, N.M., Gonzalez-Garcia, C. , Salmerón-Sánchez, M. and Altankov, G. (2011) Arrangement of type IV collagen and laminin on substrates with controlled density of –OH groups. Tissue Engineering Part A , 17(17-18), pp. 2245-2257. (doi: 10.1089/ten.tea.2010.0713 )