scholarly journals Inhibitory Activity on DNA Gyrase and Intracellular Accumulation of Quinolones: Structure-Activity Relationship of Q-35 Analogs.

1994 ◽  
Vol 17 (7) ◽  
pp. 927-930 ◽  
Author(s):  
Tatsuya ITO ◽  
Kana KOJIMA ◽  
Kinya KOIZUMI ◽  
Hiroyuki NAGANO ◽  
Takeshi NISHINO
Keyword(s):  
Inhibitory Activity ◽  
Dna Gyrase ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Intracellular Accumulation ◽  
Structure Activity ◽  
Relationship Of

Combined 3D-quantitative structure–activity relationships and topomer technology-based molecular design of human 4-hydroxyphenylpyruvate dioxygenase inhibitors

2020 ◽  
Vol 12 (9) ◽  
pp. 795-811 ◽  
Author(s):  
Yong-Xuan Liu ◽  
Shuang Gao ◽  
Tong Ye ◽  
Jia-Zhong Li ◽  
Fei Ye ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Binding Free Energy ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Type I ◽  
Quantitative Structure ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Quantitative Structure Activity Relationships ◽  
Relationship Of

Aim: 4-Hydroxyphenylpyruvate dioxygenase (HPPD) has attracted increasing attention as an important target against tyrosinemia type I. This paper aimed to explore the structure–activity relationship of HPPD inhibitors with pyrazole scaffolds and to design novel HPPD inhibitors. Methodology & results: The best 3D-quantitative structure–activity relationships model was established by two different strategies based on 40 pyrazole scaffold-based analogs. Screening of molecular fragments by topomer technology, combined with molecular docking, 14 structures were identified for potential human HPPD inhibitory activity. Molecular dynamics results demonstrated that all the compounds obtained bound to the enzyme and possessed a satisfactory binding free energy. Conclusion: The quantitative structure–activity relationship of HPPD inhibitors of pyrazole scaffolds was clarified and 14 original structures with potential human HPPD inhibitory activity were obtained.

Quantitative Structure-Activity Relationship of Substituted Benzoquinones as Inhibitors of Photosynthetic Electron Transport

1978 ◽  
Vol 33 (9-10) ◽  
pp. 695-703 ◽  
Author(s):  
Walter Oettmeier ◽  
Susanne Reimer ◽  
Klaus Link
Keyword(s):  
Inhibitory Activity ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Quantitative Structure Activity Relationship ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Quantitative Structure ◽  
Structure Activity ◽  
Alkyl Side Chains ◽  
Relationship Of

Abstract 1.4-benzoquinones have been tested for their inhibitory activity on photosynthetic NADP+ reduction by chloroplasts. Benzoquinones with one or two branched alkyl side chains are inhibitors of electron flow. Inhibitory activity can be highly increased if one - and even more if two - halogen substitutents are introduced into the quinone moiety. Iodine substitution yields a better inhibitor than bromine than chlorine. A quantitative structure activity relationship according to a bilinear model, as developed by Kubinyi, with the lipophilicity as the only parameter could be established.

Structure-activity relationship of a novel pentapeptide with cancer cell growth-inhibitory activity

2010 ◽  
Vol 16 (5) ◽  
pp. 242-248 ◽  
Author(s):  
Masakatsu Kamiya ◽  
Keisuke Oyauchi ◽  
Yoshinori Sato ◽  
Takuya Yokoyama ◽  
Mofei Wang ◽  
...  
Keyword(s):  
Cell Growth ◽  
Cancer Cell ◽  
Inhibitory Activity ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Cancer Cell Growth ◽  
Structure Activity ◽  
Growth Inhibitory ◽  
Growth Inhibitory Activity ◽  
Relationship Of

scholarly journals Structure–Activity Relationship and Molecular Docking of a Kunitz-Like Trypsin Inhibitor, Kunitzin-AH, from the Skin Secretion of Amolops hainanensis

Pharmaceutics ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 966
Author(s):  
Yuqing Chen ◽  
Xinping Xi ◽  
Chengbang Ma ◽  
Mei Zhou ◽  
Xiaoling Chen ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Inhibitory Activity ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Skin Secretion ◽  
Site Mutation ◽  
Structure Activity ◽  
Hydrophilic Residues ◽  
Inhibitory Drug ◽  
Relationship Of

Kunitz-like trypsin inhibitors are one of the most noteworthy research objects owing to their significance in pharmacological studies, including anticarcinogenic activity, obesity regulation and anticoagulation. In the current study, a novel Kunitz-like trypsin inhibitor, Kunitzin-AH, was isolated from the skin secretion of Amolops hainanensis. The novel peptide displayed a modest trypsin inhibitory activity with the inhibitor constant (Ki) value of 1.18 ± 0.08 µM without inducing damage to healthy horse erythrocytes. Then, a series of shortened variants of Kunitzin-AH were designed by truncating a peptide loop and site mutation inside the loop to illustrate the structure–activity relationship of the trypsin inhibition function. Among the variants, a significant decrease was observed for the Cys-Cys loop domain, while the extension of an Arg at N-terminus (RCKAAFC) retained the inhibitory activity, indicating that the -RCK-motif is essential in forming the reactive domain for exerting the inhibitory activity. Furthermore, substitutions of Ala by hydrophobic or hydrophilic residues decreased the activity, indicating suitable steric hindrance provides convenience for the combination of trypsin. Additionally, the conformational simulation of the analogues processed with Chimera and Gromacs and further combination simulations between the peptides and trypsin conducted with HDOCK offered a potential opportunity for the natural trypsin inhibitory drug design. The truncated sequence, AH-798, may be a good replacement for the full-length peptide, and can be optimized via cyclization for further study.

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