Zein, as one of the natural and GRAS proteins in plant, is renewable, nontoxic, biocompatible and biodegradable. Over the past decade, many research efforts have been devoted to zein-based biomaterials for several industrial applications. Combining with research experiences in our research group, the preparation methods, characterizations and pharmaceutical applications of zein-based nanoparticles were summarized in this review. Zein NPs with different particle nanostructures have been prepared by chemical crosslinking, desolvating, dispersing and micromixing strategies. The pharmaceutical applications of zein NPs are mainly focus on the drug delivery. Zein NPs can improve the drug stability, increase the oral bioavailability, control the drug release and enhance the drug targeting, thereby improving the pharmaceutical effect effectively. More efforts are required to analyze the relationship among preparation methods, particle nanostructures and pharmaceutical properties in virtue of quality by design approach, and further promote the scale-up production and clinical application of zein NPs.
To
overcome the identification challenge of low-abundance lysine
acetylation (Kac), a novel approach based on a molecularly imprinted
polymer (MIP) was developed to improve the extraction capacity of
Kac peptides in real samples. Green deep eutectic solvents (DESs)
were introduced and used as one of the synergistic functional monomers
with zinc acrylate (ZnA). Glycine–glycine–alanine–lysine(ac)–arginine
(GGAKacR) was chosen as a template and N,N′-methylenbisacrylamide (MBAA) was used as a cross-linker.
The obtained GGAKacR-MIP had excellent selectivity for the template
with an imprinting factor (IF) of up to 21.4. The histone digest addition
experiment demonstrated that GGAKacR-MIP could successfully extract
GGAKacR from a complex sample. Finally, the application to the extraction
of Kac peptides from mouse liver protein digestion was studied in
detail. The number of Kac peptides and Kac proteins identified was
130 and 110, which were 3.71-fold and 3.93-fold higher than those
of the untreated sample. In addition, the number of peptides and proteins
identified after treatment increased from 5535 and 1092 to 17 149
and 4037 (3.10-fold and 3.70-fold, respectively). The results showed
that the obtained MIP may provide an effective technical tool for
the identification of Kac-modification and peptide fractionation,
as well as a potential approach for simultaneously identifying post-translational-modified
proteomic and proteomic information.
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