Learning from Synthetic Models of Extracellular Matrix; Differential Binding of Wild Type and Amyloidogenic Human Apolipoprotein A-I to Hydrogels Formed from Molecules Having Charges Similar to Those Found in Natural GAGs

dc.creatorRosu, Silvana Antonia
dc.creatorToledo, Leandro
dc.creatorUrbano, Bruno F.
dc.creatorSánchez, Susana A.
dc.creatorCalabrese, Graciela C.
dc.creatorTricerri, María Alejandra
dc.date2017-08
dc.date2022-09-13T12:13:42Z
dc.date.accessioned2023-07-15T05:13:36Z
dc.date.available2023-07-15T05:13:36Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/141951
dc.identifierissn:1875-8355
dc.identifierissn:1572-3887
dc.identifierissn:1573-4943
dc.identifierissn:0277-8033
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7472560
dc.descriptionAmong other components of the extracellular matrix (ECM), glycoproteins and glycosaminoglycans (GAGs) have been strongly associated to the retention or misfolding of different proteins inducing the formation of deposits in amyloid diseases. The composition of these molecules is highly diverse and a key issue seems to be the equilibrium between physiological and pathological events. In order to have a model in which the composition of the matrix could be finely controlled, we designed and synthesized crosslinked hydrophilic polymers, the so-called hydrogels varying the amounts of negative charges and hydroxyl groups that are prevalent in GAGs. We checked and compared by fluorescence techniques the binding of human apolipoprotein A-I and a natural mutant involved in amyloidosis to the hydrogel scaffolds. Our results indicate that both proteins are highly retained as long as the negative charge increases, and in addition it was shown that the mutant is more retained than the Wt, indicating that the retention of specific proteins in the ECM could be part of the pathogenicity. These results show the importance of the use of these polymers as a model to get deep insight into the studies of proteins within macromolecules.
dc.descriptionInstituto de Investigaciones Bioquímicas de La Plata
dc.formatapplication/pdf
dc.format374-383
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by/4.0/
dc.rightsCreative Commons Attribution 4.0 International (CC BY 4.0)
dc.subjectMedicina
dc.subjectAmyloidosis
dc.subjectHuman apolipoprotein A-I
dc.subjectSynthetic hydrogels
dc.subjectExtracellular matrix
dc.titleLearning from Synthetic Models of Extracellular Matrix; Differential Binding of Wild Type and Amyloidogenic Human Apolipoprotein A-I to Hydrogels Formed from Molecules Having Charges Similar to Those Found in Natural GAGs
dc.typeArticulo
dc.typeArticulo


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