TY - JOUR
T1 - Surfaces Mimicking Glycosaminoglycans Trigger Different Response of Stem Cells via Distinct Fibronectin Adsorption and Reorganization
AU - Araújo, Ana R.
AU - Soares Da Costa, Diana
AU - Amorim, Sara
AU - Reis, Rui L.
AU - Pires, Ricardo A.
AU - Pashkuleva, Iva
N1 - Publisher Copyright:
© 2016 American Chemical Society.
PY - 2016/10/26
Y1 - 2016/10/26
N2 - 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 are 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.
AB - 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 are 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.
KW - adipose-derived stem cells
KW - atomic force microscopy (AFM)
KW - multiparametric surface plasmon resonance (MP-SPR)
KW - quartz crystal microbalance with dissipation (QCM-D)
KW - self-assembling monolayers
UR - http://www.scopus.com/inward/record.url?scp=84993994713&partnerID=8YFLogxK
U2 - 10.1021/acsami.6b04472
DO - 10.1021/acsami.6b04472
M3 - Article
C2 - 27714997
SN - 1944-8244
VL - 8
SP - 28428
EP - 28436
JO - ACS Applied Materials & Interfaces
JF - ACS Applied Materials & Interfaces
IS - 42
ER -