Purification, Structural Characterization, and Bioactivity of <i>Amaranthus hypochondriacus</i> Lectin
Maria Fernanda Resendiz-Otero,
Aurea Bernardino-Nicanor,
Olivia Lugo-Magaña,
Gabriel Betanzos-Cabrera,
Leopoldo González-Cruz,
José A. Morales-González,
Gerardo Acosta-García,
Eduardo Fernández-Martínez,
Arturo Salazar-Campos,
Carmen Valadez-Vega
Affiliations
Maria Fernanda Resendiz-Otero
Departamento de Ingeniería Bioquímica, Instituto Tecnológico de Celaya, Av. Tecnológico y A. García Cubas S/N, Apartado Postal 57, Celaya 38010, Mexico
Aurea Bernardino-Nicanor
Departamento de Ingeniería Bioquímica, Instituto Tecnológico de Celaya, Av. Tecnológico y A. García Cubas S/N, Apartado Postal 57, Celaya 38010, Mexico
Olivia Lugo-Magaña
Preparatoria Número 1, Universidad Autónoma del Estado de Hidalgo, Av. Benito Juárez S/N, Constitución, Pachuca de Soto 42060, Mexico
Gabriel Betanzos-Cabrera
Área Académica de Nutrición, Instituto de Ciencias de la Salud, Universidad Autónoma del Estado de Hidalgo, Pachuca Hidalgo 42113, Mexico
Leopoldo González-Cruz
Departamento de Ingeniería Bioquímica, Instituto Tecnológico de Celaya, Av. Tecnológico y A. García Cubas S/N, Apartado Postal 57, Celaya 38010, Mexico
José A. Morales-González
Laboratorio de Medicina de Conservación, Escuela Superior de Medicina, Instituto Politécnico Nacional, México, Plan de San Luis y Díaz Mirón, Col. Casco de Santo Tomás, Del. Miguel Hidalgo, Ciudad de Mexico 11340, Mexico
Gerardo Acosta-García
Departamento de Ingeniería Bioquímica y Ambiental, Tecnológico Nacional de México/IT de Celaya, Antonio-García Cubas Pte #600 Esq. Av. Tecnológico, Celaya 38010, Mexico
Eduardo Fernández-Martínez
Laboratory of Medicinal Chemistry and Pharmacology, Centro de Investigación en Biología de la Reproducción, Área Académica de Medicina, Instituto de Ciencias de la Salud, Universidad Autónoma del Estado de Hidalgo, Pachuca Hidalgo 42113, Mexico
Arturo Salazar-Campos
Área Académica de Medicina, Instituto de Ciencias de la Salud, Universidad Autónoma del Estado de Hidalgo, Pachuca Hidalgo 42113, Mexico
Carmen Valadez-Vega
Área Académica de Medicina, Instituto de Ciencias de la Salud, Universidad Autónoma del Estado de Hidalgo, Pachuca Hidalgo 42113, Mexico
Lectin extracted from Amaranthus hypochondriacus was purified using an affinity column with an agarose-fetuin matrix specific to the lectin of interest. Purification was confirmed by SDS-PAGE, revealing a single protein band with a molecular mass of 34.4 kDa. A hemagglutination assay showed that the lectin had a higher affinity for human type A erythrocytes, and its hemagglutinating activity was inhibited only by fetuin, not by mono-, di-, or trisaccharides. This demonstrated the lectin’s selectivity for the N-acetylgalactosamine present on the surface of type A erythrocytes and fetuin. Amaranth lectin exhibited antioxidant activity, which was attributed to the phenolic compounds, amino acids, and specific peptides within the protein structure that are known for their antioxidant properties. Infrared (IR) spectroscopy provided a structural analysis and confirmed lectin glycosylation, a crucial factor in its stability and its ability to bind specific glycans on cell surfaces. Cu2+, Mn2+, and Zn2+ ions were found in the lectin, and these ions were strongly bound to the protein, as dialysis against ethylenediaminetetraacetic acid (EDTA) did not remove them. pH and temperature influenced lectin stability, with higher hemagglutinating activity observed at pH 7, and it remained thermostable at 25 °C.
