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Updated: May 28, 2026
Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
Published on: September 20, 2017
Elucidating the self-assembly of prolamin-derived peptide nanoparticles prepared by enzymatic hydrolysis:
Mingxi Liu1, Boran Wang1, Xudong Yang1
1Beijing Key Laboratory of Functional Food From Plant Resources, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China; Center of Food Colloids and Delivery for Functionality, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
Abstract:
Enzymatic hydrolysis has recently emerged as a novel approach for nanoparticle preparation to overcome problems in natural prolamin-based nanoparticles. This study investigated the self-assembly properties, quercetin loading, and intestinal absorption ability of gliadin (GPNs) and zein peptide nanoparticles (ZPNs) prepared by pepsin-trypsin. GPNs had a smaller particle size as well as homogeneous size distribution due to lower molecular weight and balanced amphiphilicity. The higher surface hydrophobicity and hydrogen bonds rendered GPNs higher loading capacity of quercetin compared to ZPNs. Both GPNs-Q and ZPNs-Q demonstrated robust thermal stability, however, GPNs-Q showed superior storage stability, whereas ZPNs-Q exhibited enhanced ionic stability. GPNs and ZPNs both improved the quercetin retention, especially during intestinal digestion (about 90%). Furthermore, GPNs showed higher penetrability in mucus and enhanced cellular uptake due to superior amphiphilicity and charged properties. These findings provided a crucial foundation for the rational design of prolamin-based peptide nanocarriers, broadening the application of prolamin.
