دانلود رایگان مقاله حرارت و PH ناشی از تغییرات کنفورماسیونی مساحت سطح بدن

Abstract

Aggregation and gelation of globular proteins can be an advantage to generate new forms of nanoscale biomaterials based on the fibrillar architecture. Here, we report results obtained by exploiting the proteins' natural tendency to self-organize in 3D network, for the production of new material based on BSA for medical application. In particular, at five different pH values the conformational and structural changes of the BSA during all the steps of the thermal aggregation and gelation have been analyzed by FTIR spectroscopy. The macroscopic mechanical properties of these hydrogels have been obtained by rheological measurements. The microscopic structure of the gels have been studied by AFM and SEM images to have a picture of their different spatial arrangement. Finally, the use of the BSA hydrogels as scaffold has been tested in two different cell cultures.

4. Conclusions

The main aim of the present work has been to determine the best experimental conditions to obtain hydrogels of protein aggregates of BSA at different pH and concentration. In particular, at different pH, we have analyzed the conformational and structural changes of the protein during all the steps of the thermal aggregation and gelation. The mechanical properties of the diverse hydrogels fully agreed with spectroscopic results. Hydrogels morphologies, seen by AFM and SEM techniques, suggested that different arrangement of the protein aggregates lead to different hydrogels network with peculiar properties. The biological tests demonstrated that these gels did not affect the viability of two different cell model systems. Finally, our results indicated that it is possible to modulate the final texture of the hydrogels by tuning the pH value for appropriate tissue engineering applications.