Lectins are GPs that bind with high specificity to certain mono- or oligosaccharides. Seaweeds are good sources of novel lectins of low MW, especially red seaweeds
[5]. The functions of lectins include gamete recognition and reproductive cell fusion, as well as defense against pathogens
[5][6]. Lectins can be classified into four main groups: chitin-binding lectins, legume lectins, type-2 ribosome-inactivating proteins, and mannose-binding lectins
[7]. In the case of seaweeds, the great majority of these proteins are mannose-binding, which are the major type of glycans found in them
[2]. Likewise, relevant seaweed lectins are mannose-specific lectins, which show high binding affinity with these residues
[8]. This property allows them to “agglutinate” particles containing these residues, as is the case of bacterial, viral, or eukaryote cell surface GPs
[9]. One example is griffithsin, obtained from red
Griffithsia sp. seaweeds, which has been described with diverse biological properties
[10]. Due to these pharmacological properties, their characterization and isolation are a focus of research in medicine, molecular biology, or biochemistry. However, despite advances in the chemical characterization of seaweed lectins, additional information is still needed for a deeper understanding of their molecular structures, binding affinities, and possible biological functions for further applications
[11].