Utilize este identificador para referenciar este registo: http://hdl.handle.net/1822/43697

TítuloSurfaces mimicking glycosaminoglycans trigger different response of stem cells via distinct fibronectin adsorption and reorganization
Autor(es)Araújo, A. R.
Costa, Diana Soares da
Amorim, Sara
Reis, R. L.
Pires, R. A.
Pashkuleva, I.
Palavras-chaveAdipose-derived stem cells
Atomic force microscopy (AFM)
Multiparametric surface plasmon resonance (MP-SPR)
Quartz crystal microbalance with dissipation (QCM-D)
Self-assembling monolayers
RevistaACS Applied Materials and Interfaces
CitaçãoAraújo A. R., Soares da Costa D., Amorim S., Reis R. L., Pires R. A., Pashkuleva I. Surfaces mimicking glycosaminoglycans trigger different response of stem cells via distinct fibronectin adsorption and reorganization, Acs Applied Materials & Interfaces, Vol. 8, Issue 42, pp. 28428 - 28436, doi:10.1021/acsami.6b04472, 2016
Resumo(s)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.
Versão da editorahttp://pubs.acs.org/doi/abs/10.1021/acsami.6b04472
Arbitragem científicayes
AcessoembargoedAccess (2 Years)
Aparece nas coleções:3B’s - Artigos em revistas/Papers in scientific journals

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