Aquatic Science, Biochemistry, Genetics and Molecular Biology, Structural Biology, Biotechnology
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Scopus Publications
Scopus Publications
Rational Engineering of a Floral Nectar Peptide Generates Enhanced Antimicrobial Analogs with Different Modes of Action Dário R. A. L. Mourão, João M. Matos‐Neto, Queilane L. S. Chaves, Mariana F. Oliveira, Viviane O. Silva, et al. Chemmedchem, 2026 Antibiotic resistance is a critical challenge for global public health, stimulating the search for effective therapeutic alternatives. In this context, antimicrobial peptides (AMPs) stand out as promising candidates due to their structural diversity and multiple mechanisms of action. In this study, AMPs present in the floral nectar of Nicotiana sp. were evaluated for antibacterial activity against Staphylococcus epidermidis , S. aureus , Klebsiella pneumoniae , and Pseudomonas aeruginosa . Nicotianin‐I (NI) was identified as the most active natural peptide, although with limited efficacy. Therefore, it was selected as a model for rational engineering. From its sequence, two bioinspired analogs, NI‐A and NI‐B, were developed and showed significantly increased antibacterial activity in a strain‐dependent manner, as demonstrated by planktonic growth inhibition and cell viability assays. Mechanistic analyses indicated that NI‐A acts predominantly by destabilizing bacterial membranes, while NI‐B induces oxidative stress. Structural characterization revealed improved amphipathicity and environment‐dependent folding behavior. Hemolysis assays demonstrated that only NI‐B maintains low toxicity against human erythrocytes. Overall, these results highlight rational peptide engineering as a powerful strategy to transform low‐activity natural AMPs into optimized antimicrobial candidates with defined mechanisms and therapeutic potential.
Sponge Galectins: Structure, Evolution, and Function Andressa Rocha de Oliveira Sousa, Jessica de Assis Duarte Ferreira da Ponte, Alexandre Holanda Sampaio, Celso Shiniti Nagano, Rômulo Farias Carneiro ACS Omega, 2026
Biophysical Characterization of a Carotenoprotein from Marine Sponge Tedania ignis Reveals Pigment-Dependent Stability and Antibiotic Interactions Philippe Lima Duarte, Paulo Anderson Paiva Martins, Jéssica de Assis Duarte, Manoel Ferreira da Costa Filho, Ellen Araújo Malveira, et al. Marine Drugs, 2026 Carotenoproteins from marine sponges represent an underexplored class of pigment–protein complexes with distinctive structural and functional properties. Here, we report the isolation and biophysical characterization of a blue carotenoprotein from the sponge Tedania ignis, termed Ti-CP. The protein was purified and shown to consist of two closely related isoforms with molecular masses of approximately 27–29 kDa. Reverse-phase chromatography enabled separation of the apoprotein (ApoTi-CP) and its associated carotenoids, which were identified as oxygenated carotenoids consistent with astaxanthin and mytiloxanthin. Circular dichroism analysis revealed that both Ti-CP and ApoTi-CP are dominated by β-sheet secondary structure and display highly similar conformational profiles. In contrast, dynamic light scattering demonstrated that carotenoid binding is critical for protein stability, as the native form exhibited a compact and monodisperse organization, whereas ApoTi-CP showed pronounced aggregation. Isothermal titration calorimetry revealed that Ti-CP, but not ApoTi-CP, interacts with tetracycline, oxacillin, and streptomycin, indicating that pigment-mediated stabilization modulates ligand binding. Both Ti-CP and ApoTi-CP reduced bacterial viability and biofilm formation in a strain-dependent manner and enhanced antibiotic activity, including synergistic effects against resistant bacteria. Together, these results provide a comprehensive description of a previously uncharacterized sponge carotenoprotein and highlight the dual role of carotenoids in structural stabilization and antimicrobial modulation, reinforcing the biotechnological relevance of marine pigment–protein complexes.
Antihyperglycemic and antioxidant potential of a lectin from Alsidium triquetrum in streptozotocin-induced diabetic rats Mayron Alves de Vasconcelos, Mayara Freire de Alencar Alves, Luiz Gonzaga do Nascimento Neto, Francisco Vassiliepe Sousa Arruda, Maria do Perpétuo Socorro Saldanha da Cunha, et al. Natural Product Research, 2026 This study aimed to evaluate the antihyperglycemic and antioxidant activities of the lectin isolated from Alsidium triquetrum (BTL). Diabetes was induced in Wistar rats through low-dose streptozotocin injections. Following the confirmation of hyperglycaemia, the animals were treated with 150 mM NaCl, glibenclamide, or BTL at 600 or 900 mg/kg. The efficacy of BTL treatment was assessed by measuring serum glucose, total cholesterol, triglycerides, glutathione peroxidase, catalase, and superoxide dismutase levels on days 7, 14, and 21 post-induction. On day 21, pancreas and liver tissues were excised for histopathological analysis. BTL significantly reduced serum glucose, total cholesterol, and triglyceride levels while increasing all antioxidant enzyme levels. Moreover, the histopathological analysis suggests that BTL exerts a protective effect against diabetes-induced damage in hepatic and pancreatic tissues, indicating its potential as a therapeutic agent in managing diabetes.
Structural characterization and bacterial agglutination of a new OAAH-type lectin from the marine red alga Amansia multifida J.V. Lamouroux Renata Pinheiro Chaves, Gloria Steffanne Damasio da Silva, Suzete Roberta da Silva, Vinícius Paulino Pinto Menezes, Andressa Rocha de Oliveira Sousa, et al. Journal of Applied Phycology, 2026 Lectins are carbohydrate-binding proteins involved in diverse biological processes and with increasing relevance in biotechnological applications. In this study we report the structural characterization of a lectin from the marine red alga Amansia multifida (AML). Mass spectrometry analysis revealed two major isoforms with molecular masses of 28,388 Da and 28,661 Da. The primary structure of a lectin with a molecular weight of 28,661 Da was determined by combination of N-terminal Edman degradation, tandem mass spectrometry, and RACE-PCR, revealing four tandemly repeated domains and high sequence identity with members of the OAAH ( Oscillatoria agardhii agglutinin homologous) lectin family. Notably, A. multifida belongs to the order Ceramiales, suggesting a broader taxonomic distribution for this lectin family, previously restricted to species from the order Gigartinales. Secondary and tertiary structure analyses suggested a predominantly β-sheet conformation and a β-barrel fold, characteristic of OAAH lectins. Molecular docking showed conserved recognition of mannosylated glycans, supported by the presence of the QWGGREGPI motif in all carbohydrate recognition domains. Although AML did not exhibit direct antibacterial or antibiofilm activity, it was able to agglutinate Escherichia coli and Staphylococcus aureus strains, indicating potential interactions with mannoside-rich surface glycans. These findings enhance our understanding of marine lectin diversity and highlight AML as a new lectin of OAAH family.
DVL, a Lectin from Dioclea violacea Seeds, Disturbs the Proteomic Profile of Candida krusei, Leading to Cell Death Romério R. S. Silva, Rayara J. P. Carvalho, Maria H. C. Santos, Ana L. E. Santos, Rômulo F. Carneiro, et al. Antibiotics, 2025 Background/Objectives Plant lectins have emerged as potential antifungal molecules, where the carbohydrate recognition domain (CRD) is possibly the main mode of action of these proteins. Previously, we saw that the lectin extracted from the seeds of Dioclea violacea (DVL) has anti-candida activity against Candida krusei cells by acting to inhibit ergosterol biosynthesis, cell wall deformation, and deregulation of the redox system. Methods We have now confirmed this anti-candida activity by proteomic analysis, with the expression of proteins that show us how C. krusei cells respond to this treatment. Results A total of 395 proteins were identified: 142 proteins exclusively found in untreated C. krusei cells and 245 proteins exclusive to DVL-treated cells. Eight proteins were detected in both conditions. Six displayed positive accumulation (fold change > 1.5), one exhibited negative accumulation (fold change < 0.5). We observed the expression of proteins related to cell wall remodeling; alteration of energy metabolism, suggesting a metabolic adaptation to stress; oxidative stress was responded to through the expression of proteins with antioxidant action, in addition to identifying multidrug transport proteins that are often involved in the process of antifungal resistance and sterol transport to the membrane. Conclusions Our results show the complexity of adaptive responses of C. krusei cells to treatment with DVL, elucidating new mechanisms of resistance and paving the way for the development of more effective and innovative antifungal therapies.
Afil, a Lectin from Aplysina fistularis, Exhibits Antibiofilm and Synergistic Antibacterial Activity Against Resistant Bacteria Francisco Regivanio Nascimento Andrade, João Marcelo de Sousa Silva, Jéssica de Assis Duarte, Philippe Lima Duarte, Pedro Arthur Sousa Tabosa, et al. Microorganisms, 2025 Lectins from marine sponges have emerged as promising candidates for antimicrobial strategies, particularly against biofilm-forming pathogens. In this study, we report the purification, biochemical characterization, and antibiofilm properties of a new lectin (AfiL) isolated from Aplysina fistularis. AfiL exhibited typical features of sponge lectins, including a β-sheet-rich secondary structure and a predominant oligomeric state in solution. Dynamic light scattering (DLS) analyses confirmed that AfiL predominantly exists as a well-defined oligomer at acidic and neutral pH. Sequence analysis revealed similarity to a putative collectin-like protein from sponge Desydea avara. AfiL selectively agglutinated Staphylococcus aureus strains, correlating with its preferential binding to lipoteichoic acid (LTA). The lectin demonstrated significant antibiofilm activity against S. aureus, S. epidermidis, and Escherichia coli strains, and exhibited synergistic or additive effects when combined with conventional antibiotics against a Methicillin-resistant S. aureus. Isothermal titration calorimetry (ITC) revealed a strong interaction between AfiL and porcine stomach mucin (Kd = 1.71 × 10−6 M), consistent with multivalent carbohydrate recognition. Overall, our findings highlight the potential of AfiL as a novel antibiofilm agent with species-specific modulatory effects on antibiotic activity and provide new insights into the functional versatility of sponge-derived lectins in microbial control strategies.