Peptide hydrogels: Synthesis, properties, and applications in food science

Abstract

Due to the unique and excellent biological, physical, and chemical properties of peptide hydrogels, their application in the biomedical field is extremely wide. The applications of peptide hydrogels are closely related to their unique responsiveness and excellent properties. However, its defects in mechanical properties, stability, and toxicity limit its application in the food field. In this review, we focus on the fabrication methods of peptide hydrogels through the physical, chemical, and biological stimulations. In addition, the functional design of peptide hydrogels by the incorporation with materials is discussed. Meanwhile, the excellent properties of peptide hydrogels such as the stimulus responsiveness, biocompatibility, antimicrobial properties, rheology, and stability are reviewed. Finally, the application of peptide hydrogel in the food field is summarized and prospected.

Recent advances in peptide-based bioactive hydrogels for nerve repair and regeneration: from material design to fabrication, functional tailoring and applications

“…In this section, we would like to introduce the hydrogel design, synthesis methods, and functionalization techniques of peptide hydrogels briefly, as some details on these aspects have been provided in several previous reviews. 24–26 The readers are suggested to study these reviews in order to know more about the synthesis details of peptide hydrogels.…”

Gelation Behavior and Drug Sustained-Release Properties of a Helix Peptide Organohydrogel with pH Responsiveness

“…These characteristics have made peptide gel attractive for food and biomedical applications. , Moreover, the pH-stimulated responsiveness and porous nature of gels allow them to act as a stabilizer, sensor, and carrier for the delivery and controlled release of bioactive molecules. , As the pH changes, amino acid residues release or accept protons, causing changes in hydrogen bonding, ionic interactions, and hydrophobic interactions that lead to changes in peptide structure and peptide properties, such as peptide chain conformation, configuration, surface activity, and solubility. These changes allow reversible microphase separation or self-organization of the material . The α-helix structure of peptides is formed by intramolecular interactions.…”

“…These changes allow reversible microphase separation or self-organization of the material. 14 The α-helix structure of peptides is formed by intramolecular interactions. The side chains of residues in peptide with different shapes, sizes, charges, and the external environment could affect the interactions of side chains, thus affecting the stability of the helical structure.…”

Smart Hydrogels for Tissue Regeneration

“…These soft matrices exhibit adjustable mechanical properties similar to those of biological tissues. [18,19] Hydrogels possess desirable attributes such as biocompatibility, biodegradability, high water absorption, and water retention, making them ideal for a wide range of applications across various fields, including environmental engineering, flexible sensing, and electrochemistry. [16,[20][21][22] Specifically in the biomedical sector, hydrogels are utilized in areas such as tissue engineering, [23] drug delivery, [24] wound dressing, [25] biosensors, [22] contact lenses, [26] and artificial cells.…”