Structural Analyses of DP‐1, a Protein with the Ability To Bind Gold Nanoparticles, by Using Nuclear Magnetic Resonance Spectroscopy

Abstract

AbstractGold nanoparticles (AuNPs), consisting of metallic gold, are applied in various fields owing to their characteristic physical properties. Collimonas sp. D‐25 (D‐25) is a Gram‐negative bacterium obtained from soil, compost, and other environmental materials in the Akita Prefecture. DP‐1 is a water‐soluble protein found in D‐25 that binds specifically to AuNPs and retains them with high stability. This study aimed to identify the part of DP‐1 that interacts with AuNPs and determine its 3D structure in solution using nuclear magnetic resonance spectroscopy. Peptide fragments obtained by trypsin digestion were examined for their AuNP‐binding capacity to determine the key Au‐binding domain of DP‐1. A fragment consisting of 16 amino acid residues (GHAATPEQYGVVTANK) was identified as the peptide with the highest binding activity. Structural analyses of this peptide indicated that the main chain was elongated, and negatively charged residues in the side chain were exposed on the surface by incorporating AuNPs. These results suggest that DP‐1 interacts with AuNPs through negatively charged residues and extended hydrophobic residues for protein–protein interactions. The structural data also provide new insights into biomimetic technologies.