Promiscuous binding peptides-Computational screening reveals higher-affinity peptides for gold binding beyond phage...

Area of Science:

• Nanobiotechnology
• Materials Science
• Biomaterials

Background:

• Peptides binding inorganic surfaces are vital for nanobiotechnology and biomaterials.
• Phage display is common for peptide discovery but can miss high-affinity binders due to experimental biases.

Purpose of the Study:

• To computationally assess the binding affinity of solid-binding peptides to gold (Au(111)) surfaces.
• To identify molecular determinants of peptide-gold interactions.
• To compare computational findings with experimentally derived peptide affinities.

Main Methods:

• Molecular dynamics simulations were used to analyze 46 curated solid-binding peptides.
• Binding affinity was evaluated using interaction energy, MM/PBSA, RMSD, and residue-surface distances.
• Peptides were assessed for their interaction with Au(111) surfaces.

Main Results:

• Several peptides not previously identified as gold binders exhibited stronger affinity to Au(111) than known gold-binding peptides.
• Phage display-derived peptides showed affinity, but computational screening identified superior binders.
• The study introduces "promiscuous binding peptides" for sequences with broad high-affinity surface binding.

Conclusions:

• Computational screening offers advantages over experimental methods like phage display for identifying high-affinity peptides.
• Limitations exist in experimental selection techniques for solid-binding peptides.
• This work supports the rational design of functional peptides for metal interfaces.