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<p>The <i>Terminalia catappa</i>, an economically significant tropical plant, has been found to possess a number of bioactive compounds and medicinal uses. However, best of our knowledge no information is available regarding the structural features governing the functional properties of TC seed lectin, particularly its carbohydrate-binding specificity, which prompted the present investigation. <i>Terminalia catappa</i> (TC) seed lectin was investigated to elucidate the relationship between its structure and carbohydrate-binding function using chemical modification, spectroscopic, and biophysical approaches. The results for targeted chemical modification and spectroscopic analyses to probe the roles of specific amino acid residues in the active site and carbohydrate-binding function of TC seed lectin demonstrated that modification of tryptophan and carboxylate residues markedly inhibits hemagglutination activity. Intrinsic fluorescence studies demonstrated that tryptophan residues are mainly located in a hydrophobic environment and participate directly in ligand binding. Fluorescence quenching without major spectral shifts suggested preservation of overall protein conformation, while partial protection by lactose confirmed the involvement of tryptophan in the binding site. Quenching experiments using acrylamide, cesium chloride and potassium iodide further deciphered the microenvironment of the tryptophan residues to be negatively charged. Stern -Volmer analysis suggests that the fluorescence quenching predominantly occurs through a dynamic (collisional) mechanism. Kinetic study using N-Bromo succinimide (NBS) indicated the presence of two tryptophan residues crucial for the lectin activity. Circular dichroic spectra indicated that a highly α-helical secondary structure was present in the protein molecule. The validity of these results was confirmed by statistical testing. Collectively, these findings provide molecular-level insights into the structure–function relationship of TC seed lectin which finds its potential applications in glycoscience, diagnostics, and lectin-based biotechnological and therapeutic research.</p>

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Deciphering Structural and Functional Dynamics of Terminalia catappa (TC) Seed Lectin Using Chemical and Biophysical Methods

  • 期刊论文

  • 发表日期：

    2026年8月1日

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  • Ashish Sambhaji Uzgare,
  • Fakeha Mohammed Rehan Shaikh

摘要

The Terminalia catappa, an economically significant tropical plant, has been found to possess a number of bioactive compounds and medicinal uses. However, best of our knowledge no information is available regarding the structural features governing the functional properties of TC seed lectin, particularly its carbohydrate-binding specificity, which prompted the present investigation. Terminalia catappa (TC) seed lectin was investigated to elucidate the relationship between its structure and carbohydrate-binding function using chemical modification, spectroscopic, and biophysical approaches. The results for targeted chemical modification and spectroscopic analyses to probe the roles of specific amino acid residues in the active site and carbohydrate-binding function of TC seed lectin demonstrated that modification of tryptophan and carboxylate residues markedly inhibits hemagglutination activity. Intrinsic fluorescence studies demonstrated that tryptophan residues are mainly located in a hydrophobic environment and participate directly in ligand binding. Fluorescence quenching without major spectral shifts suggested preservation of overall protein conformation, while partial protection by lactose confirmed the involvement of tryptophan in the binding site. Quenching experiments using acrylamide, cesium chloride and potassium iodide further deciphered the microenvironment of the tryptophan residues to be negatively charged. Stern -Volmer analysis suggests that the fluorescence quenching predominantly occurs through a dynamic (collisional) mechanism. Kinetic study using N-Bromo succinimide (NBS) indicated the presence of two tryptophan residues crucial for the lectin activity. Circular dichroic spectra indicated that a highly α-helical secondary structure was present in the protein molecule. The validity of these results was confirmed by statistical testing. Collectively, these findings provide molecular-level insights into the structure–function relationship of TC seed lectin which finds its potential applications in glycoscience, diagnostics, and lectin-based biotechnological and therapeutic research.