Grewal, M. Gregory; Gray, Vincent P.; Letteri, Rachel A.; Highley, Christopher B. published their research in Biomaterials Science in 2021. The article was titled 《User-defined, temporal presentation of bioactive molecules on hydrogel substrates using supramolecular coiled coil complexes》.Reference of ((1H-Benzo[d][1,2,3]triazol-1-yl)oxy)tris(dimethylamino)phosphonium hexafluorophosphate(V) The article contains the following contents:
The ability to spatiotemporally control the presentation of relevant biomols. in synthetic culture systems has gained significant attention as researchers strive to recapitulate the endogenous extracellular matrix (ECM) in vitro. With the biochem. composition of the ECM constantly in flux, the development of platforms that allow for user-defined control of bioactivity is desired. Here, we reversibly conjugate bioactive mols. to hydrogel-based substrates through supramol. coiled coil complexes that form between complementary peptides. Our system employs a thiolated peptide for tethering to hydrogel surfaces (T-peptide) through a spatially-controlled photomediated click reaction. The complementary association peptide (A-peptide), containing the bioactive domain, forms a heterodimeric coiled coil complex with the T-peptide. Addition of a disruptor peptide (D-peptide) engineered specifically to target the A-peptide outcompetes the T-peptide for binding, and removes the A-peptide and the attached bioactive motif from the scaffold. We use this platform to demonstrate spatiotemporal control of biomol. presentation within hydrogel systems in a repeatable process that can be extended to adhesive motifs for cell culture. NIH 3T3 fibroblasts seeded on hyaluronic acid hydrogels and polyethylene glycol-based fibrous substrates supramolecularly functionalized with an RGD motif demonstrated significant cell spreading over their nonfunctionalized counterparts. Upon displacement of the RGD motif, fibroblasts occupied less area and clustured on the substrates. Taken together, this platform enables facile user-defined incorporation and removal of biomols. in a repeatable process for controlled presentation of bioactivity in engineered culture systems. In the experiment, the researchers used many compounds, for example, ((1H-Benzo[d][1,2,3]triazol-1-yl)oxy)tris(dimethylamino)phosphonium hexafluorophosphate(V)(cas: 56602-33-6Reference of ((1H-Benzo[d][1,2,3]triazol-1-yl)oxy)tris(dimethylamino)phosphonium hexafluorophosphate(V))
((1H-Benzo[d][1,2,3]triazol-1-yl)oxy)tris(dimethylamino)phosphonium hexafluorophosphate(V)(cas: 56602-33-6) is a peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis.Reference of ((1H-Benzo[d][1,2,3]triazol-1-yl)oxy)tris(dimethylamino)phosphonium hexafluorophosphate(V)
Referemce:
1,2,3-Triazole – Wikipedia,
Triazoles – an overview | ScienceDirect Topics