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The field of reconstructive surgery encompasses a wide range of surgical procedures and regenerative approaches to treat various tissue types. Every surgical procedure is associated with the risk of surgical site infections, which are not only a financial burden but also increase patient morbidity. The surgical armamentarium in this area are biomaterials, particularly natural, biodegradable, biocompatible polymers, including the silk proteins fibroin (SF) and sericin (SS). Silk is known to be derived from silkworms and is mainly composed of 60–80% fibroin, which provides the structural form, and 15–35% sericin, which acts as a glue‐like substance for the SF threads. Silk proteins possess most of the desired properties for biomedical applications, including biocompatibility, biodegradability, minimal immunogenicity, and tunable biomechanical behaviour. In an effort to alleviate or even prevent infections associated with the use of biomaterials in surgery, antibacterial/antimicrobial properties have been investigated in numerous studies. In this systematic review, the following question was addressed: Do silk proteins, SF and SS, possess an intrinsic antibacterial property and how could these materials be tailored to achieve such a property? [ABSTRACT FROM AUTHOR]

While many of the traditional ABPP probes modify protein active sites and, thereby, inhibit protein function, in a related method, known as ligand-directed chemistry, covalent protein labeling is directed by ligands to generate traceless protein modification without inhibiting the protein's function. Activity-Based Protein Profiling - Celebrating the Groundbreaking Contributions of Benjamin Cravatt The review article by Adibekian and coworkers highlights recent developments in serine hydrolase activity probes with a specific focus on the reactive groups used and their applications in understanding serine hydrolase function (B. Racioppo, N. Qiu, A. Adibekian, https://doi.org/10.1002/ijch.202300016). [Extracted from the article]