Partition of porcine pancreatic lipase in ATPS composed of PEG/salt and alcohol/salt: a thermodynamic study

Muniz, Izabella de Carvalho Batista; Oliveira, Rosana Moura de; Alves, Annie Nolasco; Silva, Emília Carmem da; Santos, Beatriz Silva; Souza, Evaldo Cardozo de; Sampaio, Vanessa Santos; Costa, Angélica Ribeiro da; Bonomo, Renata Cristina Ferreira

doi:10.1007/s43153-022-00269-9

Cited by 4 publications

References 28 publications

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Inquiry lipaseoring the mechanism of pancreatic lipase inhibition by isovitexin based on multispectral method and enzyme inhibition assay

Yu,

Xing,

Jia

et al. 2024

Luminescence

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Isovitexin is a main natural flavonoid component in various plants. Currently, the inhibitory effect of isovitexin on pancreatic lipase (PL) and its mechanism have not been elucidated yet. In the present study, we investigated the inhibitory effect of isovitexin on PL, as well as its interaction mechanism, using enzyme inhibition methods, spectroscopic analysis, and molecular simulations. Results showed that isovitexin possessed significant PL inhibitory activity, with IC50 values of 0.26 ± 0.02 mM. The interaction between isovitexin and PL was dominated by static quenching, and mainly through hydrogen bonding and hydrophobic interaction forces. Analysis of fluorescence spectroscopy confirmed that isovitexin binding altered the conformation of the PL. Circular dichroism (CD) spectrum indicated that isovitexin altered the secondary structure of PL by decreasing the α‐helix content and increasing the β‐fold content. Molecular simulations further characterize the conformational changes produced by the interaction between isovitexin with PL. The performed study may provide a new insight into the inhibitory mechanism of isovitexin as a novel PL inhibitor.

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