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Updated: Jan 20, 2026
Peptide Bonds: Formation, Structure and Conformation
Facile Peptide Bond Formation: Effective Interplay between Isothiazolone Rings and Silanol Groups at Silver/Iron
Ali Maleki1, Reza Taheri-Ledari1, Jamal Rahimi1
1Catalysts and Organic Synthesis Research Laboratory, Department of Chemistry, Iran University of Science and Technology, Tehran 16846-13114, Iran.
Abstract:
Proportional to considerable progress in protein-drug conjugations, attention to the efficient peptide coupling reagents is being increased. Hence, in this study, a versatile heterogeneous nanoscale reagent is presented for chemical, biological, and medical purposes. A combination of silver and silica-coated iron oxide nanoparticles (Ag/Fe3O4) has been well functionalized with isothiazolone rings via a silver-modified Heck mechanism. An appropriate condition is provided for peptide bond formation through the surface interplay between silanol groups and the loaded isothiazolone rings. A logical mechanism including a series of successive covalent bonds onto the surface of Ag/Fe3O4 nanocomposites is suggested for this catalyzed peptide bond formation. Accurate comparisons have been made to obtain the optimum value of the nanocatalyst and suitable conditions. As an additional application, the biological activity of the desired product has also been investigated through antibacterial assay tests. The results showed that our desired product could also be used as an effective heterogeneous nanoscale antibacterial agent for different purposes. In this regard, all of the essential structural and practical analyses have been carried out and precisely interpreted.
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