Brilliant Blue G

Biomass-derived hydrogel membranes that derived from natural polymers exhibit excellent anti-fouling properties, environmental sustainability, and mol./ionic separation performance.However, their applications are significantly hindered by poor mech. strength, excessive swelling behavior, and low permeation flux.In this study, we report the polymer structures featuring topol. defects through the in-situ synthesis of copper oxychloride particles (CP, Cu₂(OH)₃Cl) within the hydrogel membranes.The functional hydrogel membrane, designated CP-CuCaAlg, was prepared using a strategy that modulates topol. defects through secondary crosslinking.Not only does this approach enhances the mech. and anti-swelling properties of the resulting membrane, it also increases the internal network spacing, thereby effectively overcoming the trade-off between the selective separation and permeation.The CP-CuCaAlg membrane exhibits exceptional dye/salt separation performance, achieving a dye rejection rate of approx. 99.0 % towards Coomassie Brilliant Blue (CBB) and Direct Red 23 (DR).Furthermore, the salt rejection rate for sodium chloride (NaCl) remains below 10.0 %, while the permeate flux achieves an impressive value of 57.63 L m^-2h^-1 bar^-1.We anticipate that our hydrogel membranes featuring the topol. defect structures and high separation efficiency will provide a promising option for the effective treatment of dye wastewater.

Bioactive peptides display a number of favorable features as therapeutics, but their usage is challenging due to the low metabolic stability and rapid renal clearance. The small-molecule protractor, which functions by the noncovalent binding with serum albumin and protection against systemic clearance, is an attractive tool to elongate peptides' half-life. Herein, we investigated coomassie brilliant blue (CBB) as a new protractor for the half-life extension of clinically relevant glucagon-like peptide 1 (GLP-1). A series of GLP-1 analogues differentiating with CBB linkers and acylation positions are described. One particularly interesting analogue (coomatide 13) exhibits sub-picomolar potency in vitro and long-term control of glucose homeostasis in mice. A protraction mechanism study reveals that CBB has a high affinity to albumin and pan-interaction with other matrix proteins, enabling to protract peptides in both systemic circulation and the subcutaneous depot. Our study demonstrates that the specific affinity to albumin is not a prerequisite for peptide protraction, and pan-binders might be advantageous.