You will be given a definition of a task first, then some input of the task.
In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".

Paragraph: Inhibitors of bacterial DD-peptidases represent potential antibiotics. In the search for alternatives to -lactams, we have investigated a series of compounds designed to generate transition state analogue structures on reaction with DD-peptidases. The compounds contain a combination of a peptidoglycan-mimetic specificity handle and a warhead capable of delivering a tetrahedral anion to the enzyme active site. The latter include a boronic acid, two alcohols, an aldehyde and a trifluoroketone. The compounds were tested against two low molecular mass class C DDpeptidases. As expected from previous observations, the boronic acid was a potent inhibitor, but, rather unexpectedly from precedent, the trifluoroketone [D--aminopimelyl-(1,1,1-trifluoro-3amino)butan-2-one] was also very effective. Taking into account competing hydration, the trifluoroketone was the strongest inhibitor of the Actinomadura R39 DD-peptidase, with a subnanomolar (free ketone) inhibition constant. A crystal structure of the complex between the trifluoroketone and the R39 enzyme showed that a tetrahedral adduct had indeed formed with the active site serine nucleophile. The trifluoroketone moiety, therefore, should be considered along with boronic acids and phosphonates, as a warhead that can be incorporated into new and effective DD-peptidase inhibitors and therefore, perhaps, antibiotics. The bacterial DD-peptidases are of considerable importance in medical practice since they are the targets of -lactam antibiotics. (1) These enzymes catalyze the final transpeptidation reaction in the biosynthesis of bacterial cell walls and are essential to bacterial survival. The -lactams, acting as mechanism-based/transition state analogue inhibitors (2-4), are precisely structured to inactivate DD-peptidases in a manner that these enzymes have been unable to escape through evolution of a hydrolytic pathway. Bacteria have, however, been able to achieve resistance to -lactams in a number of ways unrelated to DD-peptidase active site structure, and, in particular through evolution of -lactamases from DD-peptidases (2,4). The -lactamases, unlike DD-peptidases, are able to catalyze rapid -lactam hydrolysis and thus destruction of their antibiotic activity (5).
Title: Inhibition of DD-Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 DD- Peptidase NIH Public Access Author Manuscript
Output:
True