Comparative Analysis of Banana Lectins rBanLec-Like and H84T-BanLec: An In Silico and In Vitro Approach

In this study, we conducted structural and comparative analyses of two recombinant banana lectins, rBanLec-like and H84T-BanLec, using both in silico and in vitro approaches. Sequence alignment showed 91.5% identity between the lectins, with differences in 12 amino acids. Structural modeling and secondary structure analysis indicated a high degree of structural similarity, with a root mean square deviation (RMSD) of 0.382 Å, suggesting that the sequence modifications did not lead to significant structural changes. Molecular docking experiments demonstrated a strong affinity of both lectins for mannose, with rBanLec-like exhibiting a lower binding free energy (− 6.6 kcal/mol) compared to H84T-BanLec (− 4.5 kcal/mol). Molecular dynamics simulations confirmed the stability of both proteins, although rBanLec-like displayed greater conformational flexibility. Expression in Escherichia coli showed successful production of both lectins, but rBanLec-like was detected in both soluble and insoluble fractions, whereas H84T-BanLec was exclusively obtained in the soluble fraction. Both lectins significantly inhibited the growth of colorectal adenocarcinoma cells by 62.6% and 76%, respectively. These findings contribute to the structural and functional understanding of banana lectins, highlighting their potential for biotechnological and therapeutic applications.