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Effects of single-walled carbon nanotube on the conformation of human hepcidin: molecular dynamics simulation and binding free energy calculations

Non-covalent interactions of blood peptides such as Hepcidin20 and Hepcidin25 with carbon nanotubes (CNTs) have important biological effects in a wide range of biological applications. The forces that manage the thermodynamics of interaction between peptides and carbon nanotubes are identified through the analysis of the interaction between CNTs and peptides. The main driving force of the interactions is the non-bonding van der Waals' force of attractions. In addition, we investigated the effects of different parameters in order to evaluate how the nanotube affects the structure and stability of peptides. We indicate that the peptide-SWCNT interactions through free energy calculations are thermodynamically favorable. Van der Waals contribution to the interactions in Hepcidin20-SWCNT and Hepcidin25-SWCNT complexes was negative (-134.750 and -115.641 kJ/mol, respectively (, which confirmed an extremely strong non-covalent binding energy. Results revealed that the interaction between nanotubes and the peptides could lead to a substantial conformational change of the Hepcidin20 and 25 peptide domains. Furthermore, the difference of parameter amounts calculated in both peptides is related to their N-terminal, and loop regions. These results can provide insights into peptide design strategies for future applications.