Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis

Int J Biol Macromol. 2024 Jan;256(Pt 2):128230. doi: 10.1016/j.ijbiomac.2023.128230. Epub 2023 Nov 25.

Abstract

Metallo-β-lactamase (MBL) is an enzyme produced by clinically important bacteria that can inactivate many commonly used antibiotics, making them a significant concern in treating bacterial infections and the risk of having high antibiotic resistance issues among the community. This review presents a bibliometric and patent analysis of MBL worldwide research trend based on the Scopus and World Intellectual Property Organization databases in 2013-2022. Based on the keywords related to MBL in the article title, abstract, and keywords, 592 research articles were retrieved for further analysis using various tools such as Microsoft Excel to determine the frequency analysis, VOSviewer for bibliometric networks visualization, and Harzing's Publish or Perish for citation metrics analysis. Standard bibliometric parameters were analysed to evaluate the field's research trend, such as the growth of publications, topographical distribution, top subject area, most relevant journal, top cited documents, most relevant authors, and keyword trend analysis. Within 10 years, MBL discovery has shown a steady and continuous growth of interest among the community of researchers. United States of America, China, and the United Kingdom are the top 3 countries contribute high productivity to the field. The patent analysis also shows several impactful filed patents, indicating the significance of development research on the structural and functional relationship of MBL for an effective structure-based drug design (SBDD). Developing new MBL inhibitors using SBDD could help address the research gap and provide new successful therapeutic options for treating MBL-producing bacterial infections.

Keywords: Antibiotic resistance; Enzyme promiscuity; Inhibitor; Metallo-β-lactamase; Metallo-β-lactamase fold; Structure; Zinc binding.

Publication types

  • Review

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Bacterial Infections*
  • Bibliometrics
  • Drug Design
  • Humans
  • beta-Lactamases* / chemistry

Substances

  • beta-Lactamases
  • Anti-Bacterial Agents