No abstract

Objective: We aim to evaluate the potential interaction of two insect hemolymph peptides, MDF3 and MDF4, with the human androgen receptor, on the premise that the proliferative effects of the two peptides are (at least in part) a consequence of AR binding. Methods: We employed a bioinformatic approach for the prediction of protein-peptide interaction and peptide aggregation, using various in silico on-line tools such as docking servers, aggregation prediction servers and visualization and analysis software in order to evaluate our results. Results: Our evaluation indicates that MDF3 and MDF4 interact with the androgen human androgen receptor by binding to a helix shown to be involved the receptor dimerization. Out of the two peptides, MDF3 appears to form a more extensive bond network with the receptor. Conclusion: Our analysis indicates that MDF 3 and 4 may be able to activate the human androgen receptor and warrant further investigation of the potential effect on receptor function. MDF3 appears to be the most promising out of the two peptides and its interaction should be further evaluated by both computational and experimental methods.