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Interactions and Dissociation Constants of Galactomannan Rendered Cellulose Films with Concavalin A by SPR Spectroscopy
Interactions of biomolecules at interfaces are important for a variety of physiological processes. Among these, interactions of lectins with monosaccharides have been investigated extensively in the past, while polysaccharide-lectin interactions have scarcely been investigated. Here, we explore the...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7766192/ https://www.ncbi.nlm.nih.gov/pubmed/33353119 http://dx.doi.org/10.3390/polym12123040 |
Sumario: | Interactions of biomolecules at interfaces are important for a variety of physiological processes. Among these, interactions of lectins with monosaccharides have been investigated extensively in the past, while polysaccharide-lectin interactions have scarcely been investigated. Here, we explore the adsorption of galactomannans (GM) extracted from Prosopis affinis on cellulose thin films determined by a combination of multi-parameter surface plasmon resonance spectroscopy (MP-SPR) and atomic force microscopy (AFM). The galactomannan adsorbs spontaneously on the cellulose surfaces forming monolayer type coverage (0.60 ± 0.20 mg·m(−2)). The interaction of a lectin, Concavalin A (ConA), with these GM rendered cellulose surfaces using MP-SPR has been investigated and the dissociation constant K(D) (2.1 ± 0.8 × 10(−8) M) was determined in a range from 3.4 to 27.3 nM. The experiments revealed that the galactose side chains as well as the mannose reducing end of the GM are weakly interacting with the active sites of the lectins, whereas these interactions are potentially amplified by hydrophobic effects between the non-ionic GM and the lectins, thereby leading to an irreversible adsorption. |
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