3 documents found, page 1 of 1
Design of bio-based supramolecular structures through self-assembly of α-lactal...
Monteiro, Adenilson A.; Monteiro, Márcia R.; Pereira, Ricardo N.; Diniz, Renata; Costa, Angélica R.; Malcata, F. Xavier; Teixeira, José A.Bovine α-lactalbumin (α-La) and lysozyme (Lys), two globular proteins with highly homologous tertiary structures and opposite isoelectric points, were used to produce bio-based supramolecular structures under various pH values (3, 7 and 11), temperatures (25, 50 and 75 °C) and times (15, 25 and 35 min) of heating. Isothermal titration calorimetry experiments showed protein interactions and demonstrated that str...
Design of bio-based supramolecular structures through self-assembly of α-lactal...
Monteiro, Adenilson A.; Monteiro, Marcia R.; Pereira, Ricardo N.; Diniz, Renata; Costa, Angélica R.; Malcata, F. Xavier; Teixeira, J. A.Bovine α-lactalbumin (α-La) and lysozyme (Lys), two globular proteins with highly homologous tertiary structures and opposite isoelectric points, were used to produce bio-based supramolecular structures under various pH values (3, 7 and 11), temperatures (25, 50 and 75 °C) and times (15, 25 and 35 min) of heating. Isothermal titration calorimetry experiments showed protein interactions and demonstrated that str...
Design of nanostructures, obtained from assembling of α-lactalbumin and lysozym...
Monteiro, Adenilson A.; Monteiro, Márcia R.; Ramos, Óscar L.; Pereira, Ricardo; Diniz, Renata; Costa, Angélica R.; Malcata, F. X.; Teixeira, J. A.Protein assembly into supramolecular structures (e.g. aggregates, fibrils and nanotubes) is a widespread phenomenon in biological sciences. Nowadays, it is well documented that the amphiphilic properties of proteins is a driving force to their self-assembling into innovative micro- and nanostructures of high interest in the food and pharmaceutical fields. Formation of such structures is strongly dependent on ph...