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In the under taken research that is presented here, 4\u2010(1<jats:italic>H<\/jats:italic>\u2010indol\u20103\u2010yl)butanoic acid was sequentially converted into 4\u2010(1<jats:italic>H<\/jats:italic>\u2010indol\u20103\u2010yl)butanoate, 4\u2010(1<jats:italic>H<\/jats:italic>\u2010indol\u20103\u2010yl)butanohydrazide, and 5\u2010[3\u2010(1<jats:italic>H<\/jats:italic>\u2010indol\u20103\u2010yl)propyl]\u20101,2,4\u2010triazole\u20102\u2010thiol as a nucleophile. By treating aryl amines with 3\u2010bromopropanoyl chloride in a series of parallel reactions, different electrophiles were created, leading to the formation of <jats:italic>N<\/jats:italic>\u2010(aryl)\u20103\u2010bromopropanamides. After that, several electrophiles were used in the nucleophilic substitution process of <jats:bold>5<\/jats:bold> to produce the final bi\u2010heterocyclic derivative. The structural confirmation of all the synthesized compounds was done by IR, <jats:sup>1<\/jats:sup>H\u2010NMR, <jats:sup>13<\/jats:sup>C\u2010NMR, and CHN analysis data. The enzyme inhibitory effects of these bi\u2010heterocyclic propanamides were evaluated against elastase, and all these molecules were identified as potent inhibitors relative to the standard oleanolic acid with IC<jats:sub>50<\/jats:sub> value 13.453\u00a0\u00b1\u00a00.015\u00a0\u00b5M used. The kinetics mechanism was ascribed by evaluating the Lineweaver\u2013Burk plots, which revealed that compound <jats:bold>9d<\/jats:bold> inhibited elastase competitively to form an enzyme\u2013inhibitor complex. The inhibition constant <jats:italic>K<jats:sub>i<\/jats:sub><\/jats:italic> calculated from Dixon plots for this compound was 0.51\u00a0\u00b5M. Compound <jats:bold>9d<\/jats:bold>\u2019s activity (IC<jats:sub>50<\/jats:sub>\u00a0=\u00a00.142\u00a0\u00b1\u00a00.014\u00a0\u00b5M) significantly increased when a slightly bulky ethyl group was replaced for the solitary methyl group in <jats:bold>9c<\/jats:bold> at the <jats:italic>para<\/jats:italic>\u2010position. However, compound <jats:bold>9e<\/jats:bold>\u2019s activity was significantly lower (IC<jats:sub>50<\/jats:sub>\u00a0=\u00a038.338\u00a0\u00b1\u00a00.993\u00a0\u00b5M) when a more polar ethoxy group was replaced at the same <jats:italic>para<\/jats:italic>\u2010position. This was likely because of electronic considerations. These molecules also exhibited mild cytotoxicity toward red blood cell membranes, when analyzing through hemolysis. So, these molecules might be deliberated as nontoxic medicinal scaffolds for dealing with the elastase\u2010related ailments such as lung diseases, cyclic neutropenia, pruritic skin disease, and liver infection.<\/jats:p>","DOI":"10.1002\/cbdv.202401806","type":"journal-article","created":{"date-parts":[[2024,11,22]],"date-time":"2024-11-22T03:04:34Z","timestamp":1732244674000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Convergent Synthesis, Kinetics, and Computational Studies of Indole(Phenyl)Triazole Bi\u2010Heterocycles Modified With Propanamides as Elastase Inhibitors"],"prefix":"10.1002","volume":"22","author":[{"family":"Shakila","sequence":"first","affiliation":[{"name":"Department of Chemistry Government College University  Lahore Punjab Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3439-9286","authenticated-orcid":false,"given":"Muhammad 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