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Structure-activity relationships of novel anti-malarial agents. Part 2: cinnamic acid derivatives.
TLDR
Compound 3q represents an important step in the development of lead structure 1 into an anti-malarial drug candidate after replacement of the 3-phenylpropionyl moiety of the lead structure 2 by a 4-propoxycinnamic acid residue resulted in a significant improvement in antimalarial activity. Expand
Discovery of a novel lead structure for anti-malarials.
TLDR
Some structural modifications of this initial lead demonstrated the potential for further improvement of the anti-plasmodial activity of this novel class of anti-malaria agents active against multi-resistant Plasmodium falciparum strain Dd2. Expand
Exploration of novel aryl binding sites of farnesyltransferase using molecular modeling and benzophenone-based farnesyltransferase inhibitors.
TLDR
Using flexible docking of several non-thiol farnesyltransferase inhibitors known from the literature and some model compounds based on the benzophenone scaffold as well as performing GRID searches, two regions in the farnesytransferase's active site are identified which are suggested to be the postulated aryl binding sites. Expand
Structure-activity relationships of novel anti-malarial agents. Part 4: N-(3-benzoyl-4-tolylacetylaminophenyl)-3-(5-aryl-2-furyl)acrylic acid amides.
TLDR
This work has invesigated acryloyl derivatives carrying a biaryl structure consisting of a terminal aryl residue and a central 2-furyl ring and deduced that there has to be a lipophilic moiety in the para-position of the terminal phenyl residue. Expand
Non‐thiol Farnesyltransferase Inhibitors: Utilization of the Far Aryl Binding Site by 5‐Cinnamoylaminobenzophenones
TLDR
The cinnamoyl residue was designed as an appropriate substituent for the authors' benzophenone‐based AAX‐peptidomimetic compound capable of occupying the far aryl binding site. Expand
Non-thiol farnesyltransferase inhibitors: N-(4-tolylacetylamino-3-benzoylphenyl)-3-arylfurylacrylic acid amides.
TLDR
Arylfurylacryl-substituted benzophenones as non-thiol farnesyltransferase inhibitors are designed utilizing a novel aryl binding site of farnesytransferase. Expand
Non-thiol farnesyltransferase inhibitors: utilization of an aryl binding site by 5-arylacryloylaminobenzophenones.
TLDR
The 2-naphthylacryloyl residue was developed as an appropriate substituent for the benzophenone-based AAX-peptidomimetic capable of occupying this binding site, resulting in a non-thiol farnesyltransferase inhibitor with nanomolar activity. Expand
Non‐Thiol Farnesyltransferase Inhibitors: Structure‐Activity Relationships of Aralkylsubsituted Benzophenones
TLDR
A novel class of benzophenone‐based farnesyltransferase inhibitors are described exploiting a novel aryl binding region in the farnesytransferase's active site using the trimethylene spacer of the 4‐phenyl butyroyl residue of the lead structure. Expand
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