Additional file 8 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 8

Additional file 5 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 5

Additional file 7 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 7

Additional file 1 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 1

Additional file 3 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 3

Additional file 4 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 4

Additional file 2 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 2

Additional file 6 of Proteomic profiles and the function of RBP4 in endometrium during embryo implantation phases in pigs

Additional file 6

Rational Design of Sulfonyl-γ-AApeptides as Highly Potent HIV‑1 Fusion Inhibitors with Broad-Spectrum Activity

The HIV-1 epidemic has significant social and economic implications for public health. Developing new antivirus drugs to eradicate drug resistance is still urgently needed. Herein, we demonstrated that sulfonyl-γ-AApeptides could be designed to mimic MTSC22EK, one potent HIV fusion inhibitor derived from CHR. The best two sequences revealed comparable activity to MTSC22EK in an authentic HIV-1 infection assay and exhibited broad-spectrum anti-HIV-1 activity to many HIV-1 clinical isolates. Furthermore, sulfonyl-γ-AApeptides show remarkable resistance to proteolysis and favorable permeability in PAMPA-GIT and PAMPA-BBB assays, suggesting that both sequences could control HIV-1 within the central nervous system and possess promising oral bioavailability. Mechanistic investigations suggest that these sulfonyl-γ-AApeptides function by mimicking the CHR of gp41 and tightly bind with NHR, thereby inhibiting the formation of the 6-HB structure necessary for HIV-1 fusion. Overall, our results suggest that sulfonyl-γ-AApeptides represent a new generation of anti-HIV-1 fusion inhibitors. Moreover, this design strategy could be adopted to modulate many of the PPIs

Rational Design of Sulfonyl-γ-AApeptides as Highly Potent HIV‑1 Fusion Inhibitors with Broad-Spectrum Activity

The HIV-1 epidemic has significant social and economic implications for public health. Developing new antivirus drugs to eradicate drug resistance is still urgently needed. Herein, we demonstrated that sulfonyl-γ-AApeptides could be designed to mimic MTSC22EK, one potent HIV fusion inhibitor derived from CHR. The best two sequences revealed comparable activity to MTSC22EK in an authentic HIV-1 infection assay and exhibited broad-spectrum anti-HIV-1 activity to many HIV-1 clinical isolates. Furthermore, sulfonyl-γ-AApeptides show remarkable resistance to proteolysis and favorable permeability in PAMPA-GIT and PAMPA-BBB assays, suggesting that both sequences could control HIV-1 within the central nervous system and possess promising oral bioavailability. Mechanistic investigations suggest that these sulfonyl-γ-AApeptides function by mimicking the CHR of gp41 and tightly bind with NHR, thereby inhibiting the formation of the 6-HB structure necessary for HIV-1 fusion. Overall, our results suggest that sulfonyl-γ-AApeptides represent a new generation of anti-HIV-1 fusion inhibitors. Moreover, this design strategy could be adopted to modulate many of the PPIs