A Review on the Driving Forces in the Formation of Bioactive Molecules-Loaded Prolamin-Based Particles

Abstract

Prolamin-based particles loaded with bioactive molecules have attracted widespread attention from scientists due to their novel properties in chemistry, physics, and biology. In the self-assembly process of biopolymer-based nanocapsules, noncovalent interactions are the main driving forces for reducing bulk materials to the nanoscale and controlling the release of bioactive molecules. This article reviews the types of interaction forces, binding strength, binding active sites, molecular orientation, and binding affinity that affect the release profile of bioactive molecules during the preparation of protein stabilizer particles. Different preparation formulations, the use of different biopolymers, the inherent nature of the loaded bioactive molecules, and external factors (including pH, biopolymer concentration, temperature, salt, ultrasonication, and atmospheric cold plasma treatment) lead to different types and strengths of intra- and intermolecular interactions. Strategies, such as pH, ultrasonication, and atmospheric cold plasma, to change the protein conformation are key to improving the binding strength between proteins and bioactive substances or stabilizers. This review provides some guidance for scientists and technicians dedicated to improving loading efficiency, delaying release, enhancing colloidal stability, and exploring the binding behavior among proteins, stabilizers, and bioactive molecules.