Wang Y, Zou R, Zhou Y, Zheng Y, Peng C, Liu Y, Tan H, Fu Q, Ding M (2024) Unraveling mechanisms of protein encapsulation and release in coacervates via molecular dynamics and machine learning. Chem Sci doi: 10.1039/D4SC03061C
Objective: To investigate bovine serum albumin (BSA) protein encapsulation and release within polylysine/polyglutamate (PLys/PGlu) coacervates and to conduct simulations of the coacervate encapsulation of saporin, lysozyme, actin, and EGFP proteins in the LG, GL and SIM sequence to explore the potential extension of the ingredient addition sequence effect to other proteins.
Summary: Findings emphasize the importance of ingredient addition sequence in coacervate formation and encapsulation rates, attributed to preference contact between oppositely charged proteins and poly(amino acid)s. Notably, coacervates composed of b-sheet poly(amino acid)s demonstrate greater BSA encapsulation efficiency due to their reduced entropy and flexibility. The positively charged saporin and lysozyme protein exhibited the highest encapsulation efficiency when first combined with PGlu, followed by the addition of PLys.
Usage: The authors conducted simulations of the coacervate encapsulation of saporin (PR-01).
Related Products: Saporin (Cat. #PR-01)