Differential adhesion of amino acids to inorganic surfaces

Abstract

A fundamental, yet underexplored, materials system is the interface between biological molecules and inorganic surfaces. In an elemental approach to this problem, we have systematically examined the adhesion of amino acids to a series of inorganic surfaces including metals, insulators, and semiconductors. Significant differential adhesion is observed over the full complement of amino acids, determined largely by amino acid side-chain charge. Extensive mapping of the amino acid adhesion versus materials in multiple solutions is presented, with preliminary mechanisms derived from concentration and pH dependence. These results provide an empirical basis for building peptide to inorganic surface structures, and, using this adhesion data, we design inorganic nanostructures that are shown to selectively bind to prescribed primary peptide sequences.peptide adhesion ͉ semiconductors

Substrate adhesion of a nongrafted flexible polymer in a cavity

“…The requirement of higher integration scales in electronic circuits, the onset of nanosensory applications in biomedicine, but also the fascinating capabilities of modern experimental setup with its enormous potential in polymer and surface research recently led to an increasing interest at the hybrid interface of organic and inorganic matter [1,2,3,4,5]. This also includes numerous detailed studies, e.g., of polymer film wetting phenomena [6,7], pattern recognition [8,9], protein-ligand binding and docking [10,11,12], charged adsorbed polymers [13] as well as deposition and growth of polymers at surfaces [14].…”

Structural properties of small semiconductor-binding synthetic peptides

“…In a newly growing field of research, synthetic peptides are investigated for use in hybrid nanodevices, depending on their self-assembly properties [1,2]. In these studies, it is also shown that the binding of peptides on metal and semiconductor surfaces depends on the types of amino acids [3] and on the sequences of the residues in the peptide chain [4,5,6]. These experiments reveal many different interesting and important problems, which are related to general aspects of the question why and how proteins fold.…”

Functional and Selective Bacterial Interfaces Using Cross-Scaffold Gold Binding Peptides

“…Willett et al systematically tabulated single amino acid adhesion to a variety of inorganic materials, where it was noted empirically that only amino acid residues Arg, Thr, Asp, Ser, Ile, and Pro displayed much affinity for the non-oxide-forming gold surface. 47 Arginine-rich sequences have also been found in the engineered antibody work of Jain et al 48 We note that cysteine is prominently missing from this list, despite the ubiquity of the thiol-gold interaction in the field of self-assembled monolayers (SAMs) and the spectroscopic identification of the sulfur-gold bond in other cysteine-containing gold systems. 49 However, relative rankings of amino acids as gold binders in additional work (such as that of Peelle et al, 50 Fears et al 51 and Cohavi 52 ) have not displayed consistent trends.…”

“…79 While clear trends from the literature remain elusive, a simple analysis of the three-peptide sequences in the context of known gold and silicon binders was performed. If one examines the sequences for gold-binding residues based on the work of Willett and colleagues 47 (Arg, Thr, Asp, Ser, Ile, Pro), then all peptides are roughly equivalent at six potential gold-binding residues each. As determined from molecular dynamics (Fig.…”