Abstract:
Isoaspartyl peptidase, present in higher plants, animal and certain bacteria, plays a key role in
medicine, particularly in oncology. This enzyme catalyzes the cleavage of β-linked Asp
residues from the N-terminus of polypeptides, a mechanism that contributes to its protein repair
function and potential therapeutic applications. However, enzymes derived from cyanobacteria,
such as Arthrospira platensis (A.platensis), remain underexplored despite their promising
biotechnological potential. This study focuses on the characterization of an isoaspartyl
peptidase from A. platensis, analyzing its physicochemical properties, secondary structure, and
structural and functional features using bioinformatics tools. The results show that the enzyme
is stable, thermostable, hydrophilic, and acidic in nature. Analysis of the secondary structure,
conducted with PSIPRED and SOPMA, reveals a composition of 35.35% α-helices, 49.04%
disordered structures (coils), and 15.61% β-strands. The 3D model generated by AlphaFold,
compared to those obtained with LOMETS CEthreader, SWISS-MODEl, Phyre
2
and I-TASSER was selected for its high quality, validated by PROCHECK, ERRAT, and Verify
3D.Functional analysis revealed an Asparaginase_2 domain (E-value: 1.5e-107), and protein
interaction analysis identified cyanophycinas as a major partner (confidence score: 0.830).
Molecular docking showed anticancer potential, with asparagine displaying the best binding
affinity (VINA score: -5 kcal/mol). This study represents the first comprehensive in silico
characterization of isoaspartyl peptidase from Arthrospira platensis, providing detailed
information on its structural, functional, and catalytic properties. Further research is essential
to validate these results experimentally and explore the full biotechnological potential of the
enzyme.
