Surfaces Mimicking Glycosaminoglycans Trigger Different Response of Stem Cells via Distinct Fibronectin Adsorption and Reorganization

被引:10
作者
Araujo, Ana R. [1 ,2 ]
da Costa, Diana Soares [1 ,2 ]
Amorim, Sara [1 ,2 ]
Reis, Rui L. [1 ,2 ]
Pires, Ricardo A. [1 ,2 ]
Pashkuleva, Iva [1 ,2 ]
机构
[1] Univ Minho, Headquarters European Inst Excellence Tissue Engn, Res Grp Biomat Biodegradables & Biomimet 3Bs, AvePk, P-4805017 Taipas, Guimaraes, Portugal
[2] Univ Minho, ICVS PT Govt Associate Lab 3Bs, Braga, Portugal
关键词
atomic force microscopy (AFM); multiparametric surface plasmon resonance (MP-SPR); self-assembling monolayers; adipose-derived stem cells; quartz crystal microbalance with dissipation (QCM-D); SELF-ASSEMBLED MONOLAYERS; SUBSTRATUM-BOUND FIBRONECTIN; QUARTZ-CRYSTAL MICROBALANCE; EXTRACELLULAR-MATRIX; CONFORMATIONAL-CHANGES; OSTEOBLAST ADHESION; PLASMA FIBRONECTIN; INTEGRIN BINDING; CHEMISTRY; HEPARIN;
D O I
10.1021/acsami.6b04472
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
We report on the utility of a platform created by self-assembled monolayers to investigate the influence of the degree of sulfation of glycosaminoglycans (GAGs) on their interactions with fibronectin (Fn) and the impact of these interactions on the adhesion and morphology of human adipose derived stem cells (ASCs). We used the label-free QCM-D, AFM and SPR to follow the changes in the protein adlayer in close proximity to the substrates surface and QCM-D in combination with live imaging to characterize the adherent cells. Our results suggest that Fn interactions with GAGs governed by both H-bonding and electrostatic forces. Strong electrostatic interactions cause irreversible change in the protein conformation, while the weaker H-bonding only partially restricts the protein flexibility, allowing Fn reorganization and exposure of its binding sites for ASC adhesion. These findings imply that a delicate balance between these two types of forces must be considered in the design of biomaterials that mimic GAGs.
引用
收藏
页码:28428 / 28436
页数:9
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