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Haratipour, P.

Publications and source records attributed to Haratipour, P..

2 recordsLinked to original sources

PCNA Inhibition Enhances the Antitumor Activity of KRAS-Targeted Therapies in Pancreatic Cancer

Pancreatic ductal adenocarcinoma (PDAC) is an aggressive disease with a dismal prognosis. More than 90% of PDAC tumors harbor KRAS mutations, and several KRAS inhibitors, such as off-state, on-state, mutation-specific, and pan-RAS inhibitors, are being tested in preclinical and clinical settings. However, the response to these inhibitors as single agents is less than optimal, indicating the need to identify novel combination therapies to improve treatment outcomes. Proliferating cell nuclear antigen (PCNA) is a ring-shaped clamp protein that regulates DNA replication, repair, and resolution of transcription-replication conflict, which are critical processes for pancreatic cancer survival. AOH1996 is a first-in-class, selective PCNA inhibitor in Phase I trials. Here, we found that AOH1996 treatment is efficacious in various PDAC models in vitro. PCNA and KRAS are predicted to be synthetic lethal partners, and RNA sequencing of AOH1996-treated PDAC cells reveals enrichment of MAPK and PI3K signaling pathways. Combination of AOH1996 with KRAS inhibitors demonstrates strong synergy across KRAS G12C and G12D mutant models. Treatment with a combination of AOH1996 and KRAS inhibitors induces cell cycle arrest and apoptosis in PDAC cells. Robust antitumor activity of AOH1996 in combination with RMC-6236 was observed in PDAC tumoroids. In vivo, the combination of AOH1996 with sotorasib or MRTX1133 reduced tumor growth rates compared to single-agent therapy, with no impact on mouse body weight. Residual tumor analysis showed sustained pERK and Myc inhibition in the combination arm. In conclusion, combination of AOH1996 with KRAS inhibitors is a promising therapeutic strategy for KRAS-driven PDAC, warranting further clinical investigation.

cancer biology↗

Uridine Bisphosphonates Differentiate Phosphoglycosyl Transferase Superfamilies

Complex bacterial glycoconjugates are essential for bacterial survival, and drive interactions between pathogens and symbionts, and their human hosts. Glycoconjugate biosynthesis is initiated at the membrane interface by phosphoglycosyl transferases (PGTs), which catalyze the transfer of a phosphosugar from a soluble uridine diphospho-sugar (UDP-sugar) substrate to a membrane-bound polyprenol-phosphate (Pren-P). Two distinct superfamilies of PGT enzymes, denoted as polytopic and monotopic, carry out this reaction but show striking differences in structure and mechanism. With the goal of creating non-hydrolyzable mimics (UBP-sugars) of the UDP-sugar substrates as chemical probes to interrogate critical aspects of these essential enzymes, we designed and synthesized a series of uridine bisphosphonates (UBPs), wherein the diphosphate bridging oxygen of the UDP and UDP-sugar is replaced by a substituted methylene group (CXY; X/Y = F/F, Cl/Cl, (S)-H/F, (R)-H/F, H/H, CH3/CH3). These compounds, which incorporated as the conjugating sugar an N-acetylglucosamine (GlcNAc) substituent at the {beta}-phosphonate, were evaluated as inhibitors of a representative polytopic PGT (WecA from Thermotoga maritima) and a monotopic PGT (PglC from Campylobacter jejuni). Although CHF-BP most closely mimics pyrophosphate with respect to its acid/base properties, the less basic CF2-BP conjugate most strongly inhibited PglC, whereas the more basic CH2-BP analogue was the strongest inhibitor of WecA. These surprising differences indicate different modes of ligand binding for the different PGT superfamilies implicating a modified P-O- interaction with the structural Mg2+, consistent with their catalytic divergence. Furthermore, at least for the monoPGT superfamily example, this was not the sole determinant of ligand binding: the two diastereomeric CHF-BP conjugates, which feature a chiral center at the P-CHF-P{beta} carbon, exhibited strikingly different binding affinities and the inclusion of GlcNAc with the native -anomer configuration significantly improved binding affinity. UBP-sugars are a valuable tool for elucidating the structures and mechanisms of the distinct PGT superfamilies and offer a promising scaffold to develop novel antibiotic agents for the exclusively prokaryotic monoPGT superfamily. TABLE OF CONTENTS GRAPHIC O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=130 SRC="FIGDIR/small/558431v1_ufig1.gif" ALT="Figure 1"> View larger version (28K): org.highwire.dtl.DTLVardef@3479edorg.highwire.dtl.DTLVardef@130f028org.highwire.dtl.DTLVardef@1e6d4c1org.highwire.dtl.DTLVardef@199f3e2_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗