In Situ‐Forming Cross‐linking Hydrogel Systems: Chemistry and Biomedical Applications

With the development of chemical synthetic strategies and available building blocks, in situ‐forming hydrogels have attracted significant attention in the biomedical fields over the past decade. Due to their distinct properties of easy management and minimal invasiveness via simple aqueous injections at target sites, in situ‐forming hydrogels have found a broad spectrum of biomedical applications including tissue engineering, drug delivery, gene delivery, 3D bioprinting, wound healing, antimicrobial research, and cancer research. The objective of this chapter is to provide a comprehensive review of updated research methods in chemical synthesis of in situ‐forming cross‐linking hydrogel systems and their diverse applications in the biomedical fields. This chapter concludes with perspectives on the future development of in situ‐forming hydrogels to facilitate this multidisciplinary field

Further characterization of the binding of heparin to granulocyte colony-stimulating factor: Importance of sulfate groups

Heparin mediates fundamental biological mechanisms through interaction with proteins. Previously, we have shown that standard heparin binds to granulocyte colony-stimulating factor (G-CSF) with an affinity of 4.8 x 10(5) M-1. To further study the structural features in heparin that are responsible for this interaction, we studied the bindings of G-CSF and N-desulfated and 2,3-O-desulfated heparin by CZE. Results showed that the N-desulfated heparin had a similar affinity for G-CSF ((5.4 +/- 0.9) x 10(5) M-1), but the 2,3-O-desulfated heparin had a 1000-fold lower affinity ((3.4 +/- 1.2) x 10(2) M-1) in comparison to standard heparin. The results showed that 2,3-O-sulfate groups are more important than N-sulfate groups in heparin-G-CSF interaction

Studying drug-plasma protein interactions by two-injector microchip electrophoresis frontal analysis

We developed a simple, rapid, and sensitive two-injector microchip electrophoresis frontal analysis (MCE-FA) method for studying drug-plasma protein interactions. In this method, large volumes of a reference sample and drug-plasma protein mixture were simultaneously introduced into the respective sections of the microchannel through the separated injectors and then electrophoresed. Since the reference sample did not meet with the interacting species during migration, it could be used as an external standard. The interaction between heparin and HSA was quantitatively characterized as a model system. The binding constant was found to be (1.53 +/- 0.01) X 10(4) M-1