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Cutaneous leishmaniasis (CL) is the most common form of the disease which can cause malignant lesions on the skin. Vaccination for the prevention and treatment of leishmaniasis can be the most effective way to combat this disease. In this study, we designed a novel multi-epitope vaccine against Leishmania major (L. major) using immunoinformatics tools to assess its efficacy in silico. Sequences of Leish-F1 protein (TSA, Leif, and LMSTI1) of L. major were taken from GenBank. The helper T (Th) and cytotoxic T (Tc) epitopes of the protein were predicted. The final multi-epitope consisted of 18 CTL epitopes joined by AAY linker. There were also nine HTL epitopes in the structure of the vaccine construct, joined by GPGPG linker. The profilin adjuvant (the toll-like receptor 11 agonist) was also added into the construct by AAY Linker. There were 613 residues in the structure of the vaccine construct. The multi-epitope vaccine candidate was stable and non-allergic. The data obtained from the binding of final multi-epitope vaccine-TLR11 residues (band lengths and weighted scores) unveiled the ligand and the receptor high score of binding affinity. Moreover, in silico assessment of the vaccine construct cloning achieved its suitable expression in E. coli host. Based on these results, the current multi-epitope vaccine prevents L. major infection in silico, while further confirmatory assessments are required. [ABSTRACT FROM AUTHOR]

As we know, cataract disease is caused by the aggregation of crystallin proteins, such as α, β, and γ-crystallin, in the lens of the eye. Naturally, when mutations occur in γ-crystallin proteins, its binding affinity to the α-crystallin is increased, the protein with known chaperone role. Mutant γ-crystallin proteins also have a strong affinity to bind to each other and form large oligomers. The presence of these aggregates causes opacity of the lens of the eye and causes cataract disease. In this work, we aim to investigate whether peptides can prevent mutant γ-crystallin proteins from oligomerization/aggregation. Molecular docking and molecular dynamic simulations were used to determine how three putative amyloid-binding octapeptides (RVTWEGKF, RGTFEGRF, and RITFEIKF) bind to the mutant γ-crystallin protein. The results showed that RVTWEGKF had a more favorable binding energy for interaction with the mutant protein than RGTFEGRF and RITFEIKF. Also, in the presence of RVTWEGKF, mutant γ-crystallin is less likely to form protein dimers. Based on these findings, RGTFEGRF is proposed to be tested experimentally as a potential treatment against cataract disease. [ABSTRACT FROM AUTHOR]