Category: MEDICINAL CHEMSITRY, DRUG DESIGN

[NEW] K. Fukuzawa, T. Takagi, C. Watanabe et al, J. Phys. Chem. Lett. 2021, 12, 4059−4066: Intermolecular Interaction Analyses on SARS-CoV‐2 Spike Protein Receptor Binding Domain and Human Angiotensin-Converting Enzyme 2 Receptor-Blocking Antibody/Peptide Using Fragment Molecular Orbital Calculation.

[NEW] T. Kobayashi, R. Yanagita, K. Irie, Bioorg. Med. Chem. Lett. 2020, 30, 127657: Synthesis and biological activities of simplified aplysiatoxin analogs focused on the CH/π interaction.

S. Yonezawa et al., J. Med. Chem. 2012, 55, 8838-8858. doi: 10.1021/jm3011405: Conformational restriction approach to β-secretase (BACE1) inhibitors: effect of a cyclopropane ring to induce an alternative binding mode.

T. Ozawa et al., Bioorg. Med. Chem. Lett. 2011, 19, 5231-5237: CH/pi hydrogen bonds play a role in ligand recognition and equilibrium between active and inactive states of the beta2 adrenergic receptor: An ab initio fragment molecular orbital (FMO) study.

T. Ozawa et al., J. Comput. Chem. 2011, 32, 2774-2781: Importance of CH/p Hydrogen Bonds in Recognition of the Core Motif in Proline-Recognition Domains: An Ab Initio Fragment Molecular Orbital Study.

[NEW] T. Ema et al., Chem. Commun. 2010, 46, 5440–5442: Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates.

R. K. Raju et al., Phys. Chem. Chem. Phys. 2010, 12, 7117-7125: Modelling the binding of HIV-reverse transcriptase and nevirapine: an assessment of quantum mechanical and force field approaches and predictions of the effect of mutations on binding.

I.-H. Park, C. Li, J. Molec. Recogn. 2010, 23, 1-12: Characterization of molecular recognition of STAT3 SH2 domain inhibitors through molecular simulation.

T. Hart et al., Bioorg. Med. Chem. Lett. 2009, 17, 4241-4244: Fatty acid amide hydrolase inhibitors. Surprising selectivity of chiral azetidine ureas.

A. Hirabayashi et al., Bioorg. Med. Chem. 2009, 17, 284-294: Structure-activity relationship studies of 5-benzylaminoimidazo[1,2-c]pyrimidine-8-carboxamide derivatives as potent, highly selective ZAP-70 kinase inhibitors.

K. Ohta et al., Bioorg. Med. Chem. 2009, 17, 7958-7963: Novel estrogen receptor (ER) modulators: Carbamate and thiocarbamate derivatives with m-carborane bisphenol structure.

T. Ozawa et al., Bioorg. Med. Chem. 2008, 16, 10311-10318:The importance of CH/pi hydrogen bonds in rational drug design: An ab initio fragment molecular orbital study to leukocyte-specific protein tyrosine (LCK) kinase.

R. C. Yanagita et al., J. Med. Chem. 2008, 51, 46-56: Synthesis, conformational analysis, and biological evaluation of 1-hexylindolactam-V10 as a selective activator for novel protein kinase C isozymes.

T. Sugimoto et al., Bioorg. Med. Chem. 2008, 16, 650-657: Design and physicochemical properties of new fluorescent ligands of protein kinase C isozymes focused on CH/pi interaction.

G. Toth et al., Current Pharmaceutical Design 2007, 13, 3476-3493: The role and significance of unconventional hydrogen bonds in small molecule recognition by biological receptors of pharmaceutical relevance.

Y. Yamaguchi et al., J. Med. Chem. 2007, 50, 6647-6653: Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor.

H. Mukaiyama et al., Bioorg. Med. Chem. 2007, 15, 868-885: Synthesis ad c-Src inhibitory activity of imidazo[1,5-a]pyrazine derivatives as an agent for treatment of acute ischemic stroke.

K. Irie et al., Chem. Record 2005, 5, 185-195: Toward the development of new medicinal leads with selectivity for protein kinase C isozymes.

Y. Umezawa, M. Nishio, Biopolymers 2005, 79, 248-258: CH/pi hydrogen bonds as evidenced in the substrate specificity of acetylcholine esterase. [See page 'Our papers' for Abstract]

A. Varnavas et al., Eur. J. Med. Chem. 2005, 40, 563-582: Anthranilic acid based CCK1 receptor antagonists: preliminary investigation on their second 'touch point'.

Y. Nakagawa et al., J. Am. Chem. Soc. 2005, 127, 5746-5747: Indolactam-V is involved in the CH/pi interaction with Pro-11 of the PKCd C1B domain: Application for the structural optimization of the PKCd ligand.

I. Momose et al., Bioorg. Med. Chem. Lett. 2005, 15, 1867-1871: Structure-based design of derivatives of tyropeptin A as the potent and selective inhibitors of mammalian 20S proteasome.

K. Umezawa et al., Pharmacology & Therapeutics 2003, in the press: Molecular design and biological activities of protein-tyrosine phosphatase inhibitors.

H.-O. Bertrand et al., J. Med. Chem. 2002, 45, 3171-3183: Common and selective molecular determinants involved in metabolic glutamate receptor agonist activity.

L. Chen et al., Bioorg. Med. Chem. Lett. 2002, 12, 1679-1682: Focused library approach for identification of new N-acylphenylalanines as VCAM/VLA-4 antagonist.

H. Fretz et al., Curr. Pharm. Design 2000, 6, 1777-1796: Structure-based design of compounds inhibiting Grb2-SH2 mediated protein-protein interactions in signal transduction pathways.

T. Watanabe et al., Tetrahedron 2000, 56, 741-752: Structure-activity relationship and rational design of 3,4-dephostatin derivatives as protein tyrosine phosphate inhibitors.

A. Matsushima et al., J. Biochem. 2000, 128, 225-232: Edge-to-face CH/pi interaction between ligand Phe-phenyl and receptor aromatic group in the thrombin receptor activation.

M. L. Barreca et al., Bioorg. Med. Chem. Lett. 1999, 7, 2283-2292: Comparative molecular field analysis (CoMFA) and docking studies of non-nucleoside HIV-1 RT inhibitors (NNIs).

Y. Shimohigashi et al., Biopolymers 1999, 51, 9-17: Design of serine protease inhibitors with conformation restricted by amino acid side-chain-side-chain CH/pi interaction.

J. Schoepfer et al., Bioorg. Med. Chem. Lett. 1999, 9, 221-226: Highly potent inhibitors of the Grb2-SH2 domain.

T. Nose et al., J. Biochem. 1998, 124, 354-358: Interaction mode of the Phe-phenyl group of thrombin receptor-tethered ligand SFLLRNP in receptor activation.

M. F. Perutz et al., J. Am. Chem. Soc. 1986, 108, 1064-1078: Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemsitry of binding.