ABSTRACT
Most hydrogels have poor mechanical properties, severely limiting their potential applications, and numerous approaches have been introduced to fabricate more robust and durable examples. However, these systems consist of nonbiodegradable polymers which limit their application in tissue engineering. Herein, we focus on the fabrication and investigate the influence of hydrophobic segments on ionic cross-linking properties for the construction of a tough, biodegradable hydrogel. A biodegradable, poly(γ-glutamic acid) polymer conjugated with a hydrophobic amino acid, l-phenylalanine ethyl ester (Phe), together with an ionic cross-linking group, alendronic acid (Aln) resulting in γ-PGA-Aln-Phe, was initially synthesized. Rheological assessments through time sweep oscillation testing revealed that the presence of hydrophobic domains accelerated gelation. Comparing gels with and without hydrophobic domains, the compressive strength of γ-PGA-Aln-Phe was found to be six times higher and exhibited longer stability properties in ethylenediaminetetraacetic acid solution, lasting for up to a month. Significantly, the contribution of the hydrophobic domains to the mechanical strength and stability of ionic cross-linking properties of the gel was found to be the dominant factor for the fabrication of a tough hydrogel. As a result, this study provides a new strategy for mechanical enhancement and preserves ionic cross-linked sites by the addition of hydrophobic domains. The development of tough, biodegradable hydrogels reported herein will open up new possibilities for applications in the field of biomaterials.
Subject(s)
Hydrogels , Hydrophobic and Hydrophilic Interactions , Hydrogels/chemistry , Hydrogels/chemical synthesis , Cross-Linking Reagents/chemistry , Polyglutamic Acid/chemistry , Polyglutamic Acid/analogs & derivatives , Rheology , Compressive Strength , Ions/chemistry , Biocompatible Materials/chemistry , Phenylalanine/chemistry , Phenylalanine/analogs & derivativesABSTRACT
Visible light-assisted protein patterning on a solid surface was performed with phosphorylcholine (PC) polymers bearing tyrosine residues. Because of the antifouling nature of PC polymers, protein immobilisation was regiospecifically controlled, thus enabling the microfabricated surfaces to be used as immunoassay platforms.
