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Lectins: Structural Diversity, Molecular Recognition and Emerging Applications

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 20 June 2026 | Viewed by 263

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Departamento de Bioquímica, Centro de Biociências, Universidade Federal de Pernambuco, Recife 50670-901, Brazil
Interests: biochemistry; biomolecules; proteins; biological activities; protein purification; natural products
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Special Issue Information

Dear Colleagues,

Lectins are a diverse group of carbohydrate-binding proteins that are widely distributed across microorganisms, plants, and animals. These proteins are defined by the presence of at least one non-catalytic domain that selectively and reversibly binds to mono-, oligo-, or polysaccharides without chemically modifying the carbohydrate molecules themselves.

Due to their high specificity for carbohydrate moieties, lectins play a central role in numerous physiological and ecological interactions. Their ability to recognize and bind glycans gives them a broad spectrum of biological activities, including the following:

  • Agglutination and cell recognition;
  • Anthelmintic effects;
  • Anticancer potential;
  • Antifungal effects;
  • Anti-inflammatory effects;
  • Antimicrobial activity;
  • Antiviral properties;
  • Immunomodulatory activity;
  • Insecticidal activity;
  • Mitogenic effects;
  • Neuromodulatory effects;
  • Wound healing promotion.

Beyond their natural biological functions, lectins hold immense promise in biotechnology and biomedical sciences. Their specificity and versatility make them valuable tools in various applied fields, such as the following:

  • Diagnostic tools;
  • Drug delivery systems;
  • Antiviral and antibacterial therapeutics;
  • Agricultural biotechnology;
  • Bioseparation and biosensors;
  • Cancer research and treatment;
  • Vaccine development.

This Special Issue aims to explore the broad biomedical and biotechnological potential of lectins. We hope to collate studies that encompass all the areas of interest described above, though we also welcome papers that provide novel insights and emerging applications that extend beyond these areas.

Prof. Dr. Patrícia Maria Guedes Paiva
Guest Editor

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Keywords

  • lectins
  • structural diversity
  • molecular recognition
  • bioactivities
  • biomedical applications

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Published Papers (1 paper)

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Research

17 pages, 2298 KB  
Article
Lectin–Rose Bengal Conjugates for Targeted Photodynamic Inactivation of Pathogenic Bacteria
by Melad Atrash, Iryna Hovor, Marina Nisnevitch and Faina Nakonechny
Int. J. Mol. Sci. 2026, 27(2), 819; https://doi.org/10.3390/ijms27020819 - 14 Jan 2026
Abstract
The growing threat of antibiotic-resistant bacteria necessitates the development of alternative antimicrobial strategies. This study investigated the design and evaluation of novel photodynamic agents based on Rose Bengal (RB) conjugated to two plant lectins, Pisum sativum agglutinin (PSA) and Laburnum anagyroides agglutinin (LABA), [...] Read more.
The growing threat of antibiotic-resistant bacteria necessitates the development of alternative antimicrobial strategies. This study investigated the design and evaluation of novel photodynamic agents based on Rose Bengal (RB) conjugated to two plant lectins, Pisum sativum agglutinin (PSA) and Laburnum anagyroides agglutinin (LABA), for targeted photodynamic inactivation of Gram-positive and Gram-negative bacteria. Both conjugates demonstrated high singlet oxygen quantum yields compared with free RB. Antibacterial efficacy was assessed against methicillin-sensitive and methicillin-resistant Staphylococcus aureus, Escherichia coli, Pseudomonas aeruginosa, and Salmonella paratyphi B under white LED illumination. PSA-RB exhibited superior bactericidal activity against all strains, whereas LABA-RB showed strain-specific efficacy, particularly against Gram-negative species. A binary mixture of PSA-RB and LABA-RB synergistically inactivated both MSSA and MRSA at RB concentrations of 6–10 nM and light doses of 3.1–7.8 J/cm2. Complete killing of E. coli and S. paratyphi B was achieved at approximately half the RB concentrations needed for individual conjugates. PSA-RB activity primarily drove the inactivation of P. aeruginosa. Uptake studies revealed significantly enhanced accumulation of lectin-conjugated RB compared to free RB, with synergistic uptake observed for the conjugate mixture. These results suggest that lectin-based RB conjugates are effective antibacterial agents for photodynamic treatment, especially via the dual-targeting method. Full article
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