Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces (534 views)
J Colloid Interface Sci (ISSN: 0021-9797, 1095-7103electronic, 0021-9797linking), 2013 Jan 1; 389(1): 220-229.
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Paper type: Journal Article,
Impact factor: 1.646, 5-year impact factor: 2.494
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84867910557&partnerID=40&md5=4b3d1cffbd13668fda50d348f1679a4c
Keywords: Adsorption, Hydrophobic Interactions, Molecular Flexibility, Peptide, Phage Display, Surface, Adsorbed Layers, Adsorption Behavior, Biomacromolecules, Biorecognition, Gold Interface, Gold Surfaces, High Affinity, High Frequency, Hydrophobic Residues, Inorganic Surfaces, M13 Bacteriophage, Metallic Surface, Noncovalent, Noncovalent Binding, Peptide Adsorption, Peptide Sequences, Phage Displayed Peptide, Steered Molecular Dynamics, Surface Functionalization, Binding Energy, Biomolecules, Genetic Engineering, Hydrophobicity, Metallic Compounds, Surface Measurement, Dodecapeptide, Peptide Derivative, Unclassified Drug, Amino Acid Sequence, Article, Atomic Force Microscopy, Bacteriophage M13, Binding Affinity, Chemical Interaction, Chemical Structure, Circular Dichroism, Crystal Structure, Fluorescence Imaging, Isotherm, Peptide Synthesis, Physical Chemistry, Priority Journal, Screening, Surface Plasmon Resonance, Viscoelasticity, Hydrophobic And Hydrophilic Interactions, Peptide Library, Surface Properties, Ultrastructure,
Affiliations:
*** IBB - CNR ***
Interdisciplinary Research Centre on Biomaterials (CRIB), University Federico II, Piazzale Tecchio 80, 80125 Naples, Italy
Center for Advanced Biomaterials for Healthcare CRIB, Istituto Italiano di Tecnologia (IIT), Largo Barsanti e Matteucci 53, 80125 Naples, Italy
Department of Clinical and Experimental Medicine, University Magna Graecia of Catanzaro, Viale Europa, 88100 Catanzaro, Italy
Department Biological Science-School of Biotechnological Sciences, University Federico II and National Research Council, Inst. Biostructure and Bioimaging, Via Mezzocannone, 16, 80134 Naples, Italy
References:
Not available.
J Colloid Interface Sci (ISSN: 0021-9797, 1095-7103electronic, 0021-9797linking), 2013 Jan 1; 389(1): 220-229.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.646, 5-year impact factor: 2.494
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84867910557&partnerID=40&md5=4b3d1cffbd13668fda50d348f1679a4c
Keywords: Adsorption, Hydrophobic Interactions, Molecular Flexibility, Peptide, Phage Display, Surface, Adsorbed Layers, Adsorption Behavior, Biomacromolecules, Biorecognition, Gold Interface, Gold Surfaces, High Affinity, High Frequency, Hydrophobic Residues, Inorganic Surfaces, M13 Bacteriophage, Metallic Surface, Noncovalent, Noncovalent Binding, Peptide Adsorption, Peptide Sequences, Phage Displayed Peptide, Steered Molecular Dynamics, Surface Functionalization, Binding Energy, Biomolecules, Genetic Engineering, Hydrophobicity, Metallic Compounds, Surface Measurement, Dodecapeptide, Peptide Derivative, Unclassified Drug, Amino Acid Sequence, Article, Atomic Force Microscopy, Bacteriophage M13, Binding Affinity, Chemical Interaction, Chemical Structure, Circular Dichroism, Crystal Structure, Fluorescence Imaging, Isotherm, Peptide Synthesis, Physical Chemistry, Priority Journal, Screening, Surface Plasmon Resonance, Viscoelasticity, Hydrophobic And Hydrophilic Interactions, Peptide Library, Surface Properties, Ultrastructure,
Affiliations:
*** IBB - CNR ***
Interdisciplinary Research Centre on Biomaterials (CRIB), University Federico II, Piazzale Tecchio 80, 80125 Naples, Italy
Center for Advanced Biomaterials for Healthcare CRIB, Istituto Italiano di Tecnologia (IIT), Largo Barsanti e Matteucci 53, 80125 Naples, Italy
Department of Clinical and Experimental Medicine, University Magna Graecia of Catanzaro, Viale Europa, 88100 Catanzaro, Italy
Department Biological Science-School of Biotechnological Sciences, University Federico II and National Research Council, Inst. Biostructure and Bioimaging, Via Mezzocannone, 16, 80134 Naples, Italy
References:
Not available.
Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces
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 (Keq∼106M-1, binding energy ∼-8kcal/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. © 2012 Elsevier Inc.
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 (Keq∼106M-1, binding energy ∼-8kcal/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. © 2012 Elsevier Inc.
Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces
Evolutionary screening and adsorption behavior of engineered M13 bacteriophage and derived dodecapeptide for selective decoration of gold interfaces
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14 Records (14 excluding Abstracts).
Total impact factor: 49.514 (49.514 excluding Abstracts).
Total 5 year impact factor: 50.24 (50.24 excluding Abstracts).
Total impact factor: 49.514 (49.514 excluding Abstracts).
Total 5 year impact factor: 50.24 (50.24 excluding Abstracts).
534 views. Last view on Monday 07 October 2024, 17:53:28
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