Findings on the interaction of the antimicrobial peptide cecropin-melittin with a gold surface from molecular dynamics studies.
The immobilization of gold nanoparticles (AuNPs) with antimicrobial peptides (AMPs) is a new and promising way to enhance both the activity and targeting capabilities of AMPs. However, a full understanding of the adsorption process underlying these materials is still lacking. Cecropin-melittin is a peptide with a broad antimicrobial activity while displaying low hemolytic properties, whose conjugation with AuNPs has not been studied before. In this context, we report the investigation of the adsorption process of the cecropin-melittin peptide, with (CM-SH) and without (CM) cysteine at its C-terminus, onto a gold surface based on all-atom MD simulations. Our results show that the way the peptides approach the surface dictates the final conformation and the time required to achieve it in both CM-SH and CM cases. Most important, it is demonstrated that the presence of cysteine promotes a faster conformational stabilization during the lockdown regime of the CM-SH peptide, noticeably affecting this by acting as a preferential anchoring point. This investigation represents a first step in rationalizing, with atomistic detail, some experimentally observed features of CM-SH and CM immobilized gold nanoparticles.
['Ferreira|André F|AF|', 'Rai|Akhilesh|A|', 'Ferreira|Lino|L|', 'Simões|Pedro N|PN|']
D000327:Adsorption D000595:Amino Acid Sequence D054807:Cecropins D006046:Gold D008555:Melitten D053768:Metal Nanoparticles D056004:Molecular Dynamics Simulation D011485:Protein Binding D011487:Protein Conformation D013499:Surface Properties
Antimicrobial peptide Gold surface Molecular dynamics Cysteine Cecropin melittin