RT Journal Article SR Electronic T1 Molecular Aspects of C-glycosides: Interactive Analysis of C-linked Compounds With the SGLT2 Molecular Model JF Anticancer Research JO Anticancer Res FD International Institute of Anticancer Research SP 3747 OP 3754 DO 10.21873/anticanres.16559 VO 43 IS 8 A1 OHKURA, KAZUTO A1 TABATA, ATSUSHI YR 2023 UL http://ar.iiarjournals.org/content/43/8/3747.abstract AB Background/Aim: Interaction analysis between modeled human sodium/glucose cotransporter 2 (hSGLT2) and antidiabetic C-glycoside drugs, such as canagliflozin, dapagliflozin, ipragliflozin, empagliflozin, tofogliflozin, and luseogliflozin was performed. Materials and Methods: The hSGLT2 was modeled using the X-ray data of Vibrio parahaemolyticus SGLT2 (protein data bank ID=2XQ2) as a template. Conformational analyses of C-glycosides were performed using CAChe-Conflex. Interactive analyses between hSGLT2 and C-glycosides were performed using Molegro Virtual Docker. Results: Canagliflozin interacted with hSGLT2 via Asn75, Ser287, Lys321 and Gln457. Dapagliflozin interacted with six amino acids (Arg46, Arg49, Ile76, Ser78, Met216 and Ser393). Ipragliflozin (Ala69, Met596 and Gln600), empagliflozin (Ser78, Gly79, Lys154, Asp158 and Ser393), tofogliflozin (Arg49, Met216, Ala389, Ser392 and Ser393), and luseogliflozin (Arg49, Ser74, Ser78, Gly79, His80, Lys154, Asp158 and Ser393) interacted with hSGLT2 via the amino acids described in the parentheses. Conclusion: The binding mode of each C-glycoside drug to hSGLT2 was different, and structural features of each compound were revealed. The reactive base points of C-glycosides were the sugar moiety, with the sugar structure being important for hSGLT2 inhibitory action.