Peptides with an exposed arginine-glycine-aspartate (Arg-Gly-Asp, RGD) sequence targeting the integrin α β play an important role in targeted anticancer drug delivery. The interaction of multiple RGD-containing peptides and two α β molecules was studied via MD simulation. Results revealed that not all six RGD-containing peptides interact with α β and interaction strengths differed among the peptides. The specific identification sites included the guanidine group of the ARG residue in the RGD peptide and the carboxyl group of the ASP residue in integrin α β . Therefore, formation of a salt bridge between ARG and the ASP residue was the main mechanism of interaction. H-bonds also played an important role in the observed interaction. The interaction between RGD-containing peptides and α β was influenced by two factors: the relative orientation and distance between these groups. The RGD cluster, which could markedly increase the number of absorbed RGD monomers and enhance the cellular uptake of nano-medicines, was observed in this system.
Soybean bioactivity is significantly enhanced during tempeh fermentation. This study aimed to evaluate the efficacy of tempeh on colorectal cancer cells in vitro and colon precancerous lesions (aberrant crypt foci, ACF) in vivo. In the in vitro assay, tempeh water extract (WET) could inhibit the proliferation of Caco-2 cells. In the animal assay using 1,2-dimethylhydrazine (DMH)-induced Sprague–Dawley (SD) rats, 12-weeks daily feeding of tempeh could decrease the level of Clostridium perfringens in cecum contents and reduce the number of large (≥4 foci) ACF in the colon of treated rats, compared to the DMH control. By the results of TOF-MS and Edman degradation, the isolated antioxidant dipeptide, tripeptides, and tetrapeptides from WET might contain methionine, proline, and lysine. The bioactive peptides in tempeh might inhibit colon cancer by suppressing the growth of C. perfringens in the intestinal tract.
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