Inhibition of Clostridium histolyticum collagenases by phosphonamide peptide inhibitors was written by Dive, Vincent;Yiotakis, Athanasios;Nicolaou, Anna;Toma, Flavio. And the article was included in European Journal of Biochemistry in 1990.Category: alcohols-buliding-blocks This article mentions the following:
Several phosphonamide peptides having the general structure R-PO(OH)-Xaa-Yaa-Zaa were synthesized and tested for inhibition of C. histolyticum collagenase. Inhibition depended on the nature of R, Xaa, Yaa, and Zaa such that the maximal affinity (Ki = 5 nM) was observed when R = p-nitrophenylethyl, Xaa = Gly, Yaa = Pro, and Zaa = 2-aminohexanoic acid; this represents the tightest binding of inhibitor reported to date for any bacterial collagenase. Substitution of the p-nitrophenylethyl by a Me group led to a 500-fold decrease of the potency, highlighting the existence of optimal interaction between the nitrophenylethyl side chain and one subsite of the enzyme. Replacement of the NH group in glycine residue (Xaa position) by -O- or -N-CH3 produces significantly less potent inhibitors, presumably due in part to the loss of a H bond between the inhibitor and collagenase active site. These phosphonamidates are thought to be acting as transition-state analogs of the peptide substrate. In the experiment, the researchers used many compounds, for example, 2-(4-(Trifluoromethyl)phenyl)ethanol (cas: 2968-93-6Category: alcohols-buliding-blocks).
2-(4-(Trifluoromethyl)phenyl)ethanol (cas: 2968-93-6) belongs to alcohols. Alcohols are weak acids. The most acidic simple alcohols (methanol and ethanol) are about as acidic as water, and most other alcohols are somewhat less acidic. A multistep synthesis may use Grignard-like reactions to form an alcohol with the desired carbon structure, followed by reactions to convert the hydroxyl group of the alcohol to the desired functionality.Category: alcohols-buliding-blocks
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts