Titanium dioxide

N-Dodecyl-β-D-maltoside (Lauryl Maltoside) is a non-ionic detergent. N-Dodecyl-β-D-maltoside has strong adsorption on alumina, titanium dioxide and hematite. N-Dodecyl-β-D-maltoside can promote the reactivation of various proteins. N-Dodecyl-β-D-maltoside can effectively stabilize photoactive reaction center complexes (RCs) and inhibit the degradation of Rhodopseudomonas spheroides R-26 reaction center in solution. N-Dodecyl-β-D-maltoside can be used for purification and stabilization of RNA polymerase and for detection of protein-lipid interactions .

Titanium(IV) oxide is a photosensitizer and photocatalyst. Titanium(IV) oxide can be used as a pharmaceutical excipient such as a flow aid, coating agent, sunscreen, colorant, etc. Pharmaceutical excipients or pharmaceutical excipients refer to other chemical substances used in the pharmaceutical process other than the drug ingredients. Pharmaceutical excipients generally refer to inactive ingredients in pharmaceutical preparations that can improve the stability, solubility and processability of pharmaceutical preparations. Pharmaceutical excipients also affect the absorption, distribution, metabolism and elimination (ADME) process of co-administered drugs. Titanium(IV) oxide can use light energy to generate electron-hole pairs to degrade pollutants. Photons excite electrons in TiO₂ to generate active oxygen species (such as ·OH and ·O₂ ^-), thereby oxidizing and mineralizing pollutants such as organic compounds and heavy metals. TiO₂ can be used in the research of environmental remediation fields such as water treatment, air purification and self-cleaning materials .

Titanium dioxide magnetic beads are magnetic microparticle carriers whose surface is coated with titanium dioxide nanoparticles. This material is commonly used in protein digests of biological samples for the simple, convenient, efficient, highly specific, and reproducible enrichment of phosphorylated peptides. The surface properties of titanium dioxide magnetic beads make them show no significant preference for monophosphorylated or polyphosphorylated peptides, making them ideal for single-step enrichment of phosphorylated peptides in mass spectrometry-based proteomics analysis.