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A hybrid tris-bidentate neutral ligand (L) composed of a central 2,2′-bipyridine and two terminal triazolyl-pyridine chelating units connected by methylene spacers is employed to synthesize trinuclear triple-stranded side-by-side helicates of first-row transition-metal(II) ions. Three such new homometallic helicates L3M3(OTf)6[ M = Cu2+(4); Ni2+(5); Co2+(6)], along with our recently reported helicates L3Fe3(OTf)6(1), L3Zn3(OTf)6(2), and L3Fe2Zn(OTf)6(3) are taken into consideration for competitive formation and transmetalation studies. Single-crystal X-ray structures of L3Cu3(OTf)6(4) and L3Ni3(OTf)6(5) show the formation of trinuclear triple-stranded side-by-side helicates with alternating Λ and Δ chiralities at the metal ions as earlier observed in cases of L3Fe3(OTf)6(1), L3Zn3(OTf)6(2), and L3Fe2Zn(OTf)6(3). ESI-FTICR mass spectrometry and UV–vis spectroscopy studies show that helicates L3Fe3(OTf)6(1), L3Zn3(OTf)6(2), L3Fe2Zn(OTf)6(3), and L3Co3(OTf)6(6) can easily be transmetalated to helicate L3Cu3(OTf)6(4) in the presence of Cu(OTf)2. On the other hand, only a trace amount of heterometallic helicate L3Ni2Cu(OTf)6forms even after several days, when Cu(OTf)2is added to a the solution of homometallic helicate L3Ni3(OTf)6(5). Further, we have demonstrated the formation of a heterometallic helicate L3Ni2Co(OTf)6(7) from a 1:1:1 reaction mixture of L, Ni(OTf)2, and Co(OTf)2, which can also be prepared from homometallic helicate L3Co3(OTf)6(6) by transmetalation with Ni(OTf)2.

Cultivated meat production is a promising technology to generate meat while reducing the reliance on traditional animal farming. Biomaterial scaffolds are critical components in cultivated meat production, enabling cell adhesion, proliferation, differentiation, and orientation. In the present work, naturally derived glutenin was fabricated into films with and without surface patterning and in the absence of toxic cross-linking or stabilizing agents for cell culture related to cultivated meat goals. The films were stable in culture media for at least 28 days, and the surface patterns induced cell alignment and guided myoblast organization (C2C12s) and served as a substrate for 3T3-L1 adipose cells. The films supported adhesion, proliferation, and differentiation with mass balance considerations (films, cells, and matrix production). Freeze-thaw cycles were applied to remove cells from glutenin films and monitor changes in glutenin mass with respect to culture duration. Extracellular matrix (ECM) extraction was utilized to quantify matrix deposition and changes in the original biomaterial mass over time during cell cultivation. Glutenin films with C2C12s showed mass increases with time due to cell growth and new collagen-based ECM expression during proliferation and differentiation. All mass balances were compared among cell and noncell systems as controls, along with gelatin control films, with time-dependent changes in the relative content of film, matrix deposition, and cell biomass. These data provide a foundation for cell/biomaterial/matrix ratios related to time in culture as well as nutritional and textural features.