A Comprehensive Review of Self-Assembled Food Protein-Derived Multicomponent Peptides: From Forming Mechanism and Structural Diversity to Applications

被引:23
作者
Li, Yajuan [1 ]
Liu, Jingbo [1 ]
Zhang, Hui [1 ]
Shi, Xiaoxia [1 ]
Li, Shanglin [1 ]
Yang, Meng [1 ]
Zhang, Ting [1 ]
Xiao, Hang [2 ]
Du, Zhiyang [1 ]
机构
[1] Jilin Univ, Coll Food Sci & Engn, Jilin Prov Key Lab Nutr & Funct Food, Changchun 130062, Peoples R China
[2] Univ Massachusetts, Dept Food Sci, Amherst, MA 01003 USA
基金
中国国家自然科学基金;
关键词
Multicomponent peptides; Self-assembly; Enzymatichydrolysis; Noncovalent interactions; Nutraceuticalsdelivery; BETA-LACTOGLOBULIN NANOFIBRILS; ALPHA-LACTALBUMIN; WHEY-PROTEIN; ANTIOXIDANT ACTIVITY; LIMITED PROTEOLYSIS; FORMATION KINETICS; NANOSTRUCTURES; NANOTUBES; BIOAVAILABILITY; ENCAPSULATION;
D O I
10.1021/acs.jafc.3c02930
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Food protein-derived multicomponentpeptides (FPDMPs)are a naturalblend of numerous peptides with various bioactivities and multipleactive sites that can assume several energetically favorable conformationsin solutions. The remarkable structural characteristics and functionalattributes of FPDMPs make them promising codelivery carriers thatcan coassemble with different bioactive ingredients to induce multidimensionalstructures, such as fibrils, nanotubes, and nanospheres, thereby producingspecific health benefits. This review offers a prospective analysisof FPDMPs-based self-assembly nanostructures, focusing on the mechanismof formation of self-assembled FPDMPs, the internal and external stimuliaffecting peptide self-assembly, and their potential applications.In particular, we introduce the exciting prospect of constructingfunctional materials through precursor template-induced self-assemblyof FPDMPs, which combine the bioactivity and self-assembly capacityof peptides and could dramatically broaden the functional utilityof peptide-based materials.
引用
收藏
页码:11304 / 11319
页数:16
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