There is a growing interest in identifying biomacromolecules such as proteins and peptides to functionalizemetallic surfaces through noncovalent binding. One method for functionalizing materials withoutfundamentally changing their inherent structure is using biorecognition moieties. Here, we proved a generalroute to select a biomolecule adhesive motif for surface functionalization by comprehensivelyscreening phage displayed peptides. In particular, we selected a genetically engineered M13 bacteriophageand a linear dodecapeptide derived from its pIII domain for recognizing gold surfaces in a specificand selective manner. In the phage context, we demonstrated the adhesive motif was capable to adsorbon gold in a preferential way with a morphological and viscoelastic signature of the adsorbed layer as evidencedby QCM-D and AFM investigations. Out of the phage context, the linear dodecapeptide is reproduciblyfound to adhere to the gold surface, and by quantitative SPR measurements, high affinityconstants (Keq 106M1, binding energy 8 kcal/mol) were determined.We proved that the interactions occurring at gold interface were mainly hydrophobic as a consequenceof high frequency of hydrophobic residues in the peptide sequence. Moreover, by CD, molecular dynamicsand steered molecular dynamics, we demonstrated that the molecular flexibility only played a minor rolein the peptide adsorption.Such noncovalent but specific modification of inorganic surfaces through high affinity biomoleculeadsorption represents a general strategy to modulate the functionality of multipurpose metallic surfaces.

There is a growing interest in identifying biomacromolecules such as proteins and peptides to functionalize metallic surfaces through noncovalent binding. One method for functionalizing materials without fundamentally changing their inherent structure is using biorecognition moieties. Here, we proved a general route to select a biomolecule adhesive motif for surface functionalization by comprehensively screening phage displayed peptides. In particular, we selected a genetically engineered M13 bacteriophage and a linear dodecapeptide derived from its pIII domain for recognizing gold surfaces in a specific and selective manner. In the phage context, we demonstrated the adhesive motif was capable to adsorb on gold in a preferential way with a morphological and viscoelastic signature of the adsorbed layer as evidenced by QCM-D and AFM investigations. Out of the phage context, the linear dodecapeptide is reproducibly found to adhere to the gold surface, and by quantitative SPR measurements, high affinity constants (K(eq)~10(6)M(-1), binding energy ~-8 kcal/mol) were determined. We proved that the interactions occurring at gold interface were mainly hydrophobic as a consequence of high frequency of hydrophobic residues in the peptide sequence. Moreover, by CD, molecular dynamics and steered molecular dynamics, we demonstrated that the molecular flexibility only played a minor role in the peptide adsorption. Such noncovalent but specific modification of inorganic surfaces through high affinity biomolecule adsorption represents a general strategy to modulate the functionality of multipurpose metallic surfaces.

Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces.

Causa F;Iaccino E;Mimmi S;Battista E;Palmieri C;Quinto I;Scala G;Netti PA.
2013-01-01

Abstract

There is a growing interest in identifying biomacromolecules such as proteins and peptides to functionalizemetallic surfaces through noncovalent binding. One method for functionalizing materials withoutfundamentally changing their inherent structure is using biorecognition moieties. Here, we proved a generalroute to select a biomolecule adhesive motif for surface functionalization by comprehensivelyscreening phage displayed peptides. In particular, we selected a genetically engineered M13 bacteriophageand a linear dodecapeptide derived from its pIII domain for recognizing gold surfaces in a specificand selective manner. In the phage context, we demonstrated the adhesive motif was capable to adsorbon gold in a preferential way with a morphological and viscoelastic signature of the adsorbed layer as evidencedby QCM-D and AFM investigations. Out of the phage context, the linear dodecapeptide is reproduciblyfound to adhere to the gold surface, and by quantitative SPR measurements, high affinityconstants (Keq 106M1, binding energy 8 kcal/mol) were determined.We proved that the interactions occurring at gold interface were mainly hydrophobic as a consequenceof high frequency of hydrophobic residues in the peptide sequence. Moreover, by CD, molecular dynamicsand steered molecular dynamics, we demonstrated that the molecular flexibility only played a minor rolein the peptide adsorption.Such noncovalent but specific modification of inorganic surfaces through high affinity biomoleculeadsorption represents a general strategy to modulate the functionality of multipurpose metallic surfaces.
2013
There is a growing interest in identifying biomacromolecules such as proteins and peptides to functionalize metallic surfaces through noncovalent binding. One method for functionalizing materials without fundamentally changing their inherent structure is using biorecognition moieties. Here, we proved a general route to select a biomolecule adhesive motif for surface functionalization by comprehensively screening phage displayed peptides. In particular, we selected a genetically engineered M13 bacteriophage and a linear dodecapeptide derived from its pIII domain for recognizing gold surfaces in a specific and selective manner. In the phage context, we demonstrated the adhesive motif was capable to adsorb on gold in a preferential way with a morphological and viscoelastic signature of the adsorbed layer as evidenced by QCM-D and AFM investigations. Out of the phage context, the linear dodecapeptide is reproducibly found to adhere to the gold surface, and by quantitative SPR measurements, high affinity constants (K(eq)~10(6)M(-1), binding energy ~-8 kcal/mol) were determined. We proved that the interactions occurring at gold interface were mainly hydrophobic as a consequence of high frequency of hydrophobic residues in the peptide sequence. Moreover, by CD, molecular dynamics and steered molecular dynamics, we demonstrated that the molecular flexibility only played a minor role in the peptide adsorption. Such noncovalent but specific modification of inorganic surfaces through high affinity biomolecule adsorption represents a general strategy to modulate the functionality of multipurpose metallic surfaces.
Phage display; gold surface; peptide adsorption; Hydrophobic interactions; Molecular flexibility
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.12317/13174
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