Purpose: This work investigates how the model protein, bovine serum albumin (BSA), could affect the gelification process of Poloxamer 407 hydrogel and the methotrexate (MTX) release profile. Methods: The influence of BSA on the micellization behaviour of Poloxamer 407 was studied by several techniques such as differential scanning calorimetry (microDSC), dynamic light scattering (DLS), fluorescence spectroscopy and rheology. The release study of MTX loaded inside the gels in presence and in absence of BSA was performed. Results: DLS results together with microcalorimetry traces reveal that the micellization process of Poloxamer 407 is not affected by the protein as demonstrated by micellar size and thermodynamical parameters (e.g. critical micellar temperature (CMT)). The presence of BSA inside the Poloxamer 407 hydrogel (20.5% w/w, buffer phosphate 100 mM pH 7.3), loaded with MTX, has shown to delay the drug release. This behaviour occurred despite the presence of the protein has resulted in reduction of consistency of gel. Conclusion: The results suggested that kinetics of MTX release is not exclusively determined by Poloxamer 407 concentration, but other mechanisms, related to BSA, could be involved.
Effect of BSA on methotrexate release from POLOXAMER 407 hydrogel
PERINELLI, DIEGO ROMANO;PUCCIARELLI, Stefania;BONACUCINA, Giulia;CESPI, MARCO;PALMIERI, Giovanni Filippo
2013-01-01
Abstract
Purpose: This work investigates how the model protein, bovine serum albumin (BSA), could affect the gelification process of Poloxamer 407 hydrogel and the methotrexate (MTX) release profile. Methods: The influence of BSA on the micellization behaviour of Poloxamer 407 was studied by several techniques such as differential scanning calorimetry (microDSC), dynamic light scattering (DLS), fluorescence spectroscopy and rheology. The release study of MTX loaded inside the gels in presence and in absence of BSA was performed. Results: DLS results together with microcalorimetry traces reveal that the micellization process of Poloxamer 407 is not affected by the protein as demonstrated by micellar size and thermodynamical parameters (e.g. critical micellar temperature (CMT)). The presence of BSA inside the Poloxamer 407 hydrogel (20.5% w/w, buffer phosphate 100 mM pH 7.3), loaded with MTX, has shown to delay the drug release. This behaviour occurred despite the presence of the protein has resulted in reduction of consistency of gel. Conclusion: The results suggested that kinetics of MTX release is not exclusively determined by Poloxamer 407 concentration, but other mechanisms, related to BSA, could be involved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
