Selection and characteristics of peptides that bind thermally grown silicon dioxide films

Eteshola, Edward; Brillson, L. J.; Lee, Stephen Craig

doi:10.1016/j.bioeng.2005.09.004

Cited by 55 publications

(58 citation statements)

References 17 publications

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“…Histidines have also been found abundant in earlier phage display binding studies directed toward other nonmetalloprotease systems (36)(37)(38). These observations led us to hypothesize that the histidines in the WQPDTAHHWATL peptide are not directly involved in PSMA binding.…”

Section: Discussionmentioning

confidence: 90%

A Dimeric Peptide That Binds Selectively to Prostate-Specific Membrane Antigen and Inhibits its Enzymatic Activity

et al. 2006

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Prostate-specific membrane antigen (PSMA) is highly expressed by both normal and malignant prostate epithelial cells and by the neovasculature of many tumor types; however, it is not expressed by normal endothelial cells or other normal tissues. PSMA, therefore, represents an attractive candidate for selectively targeted therapies for prostate and/or other solid tumors. As an alternative approach to antibody-based anti-PSMA therapies, small peptides that bind selectively to PSMA-producing cells can be used to deliver cytotoxic drugs, protein toxins, and viruses selectively to malignant sites while minimizing systemic toxicity to normal tissues. Small peptides are relatively inexpensive to produce, not immunogenic, and easily coupled to cytotoxic agents. In the present study, a random phage library consisting of linear 12 amino acid peptides was used to identify peptides that bound selectively to PSMA. From a series of monomeric peptides, one with the sequence WQPDTAHHWATL was used to show binding of soluble peptide to PSMA. A dimeric version of this peptide showed markedly enhanced binding to soluble PSMA and an IC 50 of 2.2 Mmol/L for inhibition of PSMA enzymatic activity. Fluorescently labeled dimeric peptide bound selectively to PSMA-producing prostate cancer cells in vitro with no significant binding to non-PSMA-producing cells. Molecular modeling of the dimeric peptide revealed that histidine residues in close vicinity can efficiently coordinate a divalent ion and hold the peptide in a favorable configuration for binding and subsequent inhibition. These dimeric peptides, therefore, represent putative PSMA-selective targeting agents that are currently being evaluated for selective binding in vivo. (Cancer Res 2006; 66(18): 9171-7)

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Section: Discussionmentioning

confidence: 90%

A Dimeric Peptide That Binds Selectively to Prostate-Specific Membrane Antigen and Inhibits its Enzymatic Activity

et al. 2006

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“…There are also a number sequences selected for various materials by other groups (Gaskin et al 2000;Feldheim & Eaton 2007;Guo et al 2007). The ones selected via cell surface display include gold (Brown 1997) and zinc oxide (Kjaergaard et al 2000), whereas phage display selected ones are for their affinity towards gallium arsenide (Whaley et al 2000), silica (Naik et al 2002a;Eteshola et al 2005), silver (Naik et al 2002b), zinc sulphide (Lee et al 2002a), calcite (Li et al 2002), cadmium sulphide (Mao et al 2003) and titanium oxide (Sano et al 2005). Some biocombinatorially selected peptides have been used to assemble inorganic particles (Whaley et al 2000;Lee et al 2002a,b;Mao et al 2003;Matthes et al 2008) or to control nucleation of the compounds that they were selected for (Li et al 2002;Naik et al 2002a,b;Tullman et al 2008).…”

Section: Genetic Selection and Directed Evolution Of Solid-binding Pementioning

confidence: 99%

Molecular biomimetics: nanotechnology and bionanotechnology using genetically engineered peptides

Tamerler

Sarıkaya

2009

Phil. Trans. R. Soc. A.

101

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Nature provides inspiration for designing materials and systems that derive their functions from highly organized structures. Biological hard tissues are hybrid materials having inorganics within a complex organic matrix, the molecular scaffold controlling the inorganic structures. Biocomposites incorporate both biomacromolecules such as proteins, lipids and polysaccharides, and inorganic materials, such as hydroxyapatite, silica, magnetite and calcite. The ordered organization of hierarchical structures in organisms begins via the molecular recognition of inorganics by proteins that control interactions and is followed by the highly efficient self-assembly across scales. Following the molecular biological principle, proteins could also be used in controlling materials formation in practical engineering via self-assembled, hybrid, functional materials structures. In molecular biomimetics, material-specific peptides could be the key in the molecular engineering of biology-inspired materials. With the recent developments of nanoscale engineering in physical sciences and the advances in molecular biology, we now combine genetic tools with synthetic nanoscale constructs to create a novel methodology. We first genetically select and/or design peptides with specific binding to functional solids, tailor their binding and assembly characteristics, develop bifunctional peptide/protein genetic constructs with both material binding and biological activity, and use these as molecular synthesizers, erectors and assemblers. Here, we give an overview of solid-binding peptides as novel molecular agents coupling bioand nanotechnology.

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“…Although there are limitations to this approach, 60,61 a number of metal-binding peptides (M-BPs) [62][63][64][65] and metal oxide-binding peptides (MO-BPs) 46,58,[66][67][68][69][70] have been identified that have either been shown to have an affinity for the surface they were isolated from or have been shown to influence the growth of their respective metal or metal oxide. The identification of ZnO-binding peptides (ZnO-BPs) and understanding how they adhere to the surface of ZnO is potentially useful for the construction of artificial biomaterials, medical implants, and biosensors where biocompatibility is required.…”

Section: Introductionmentioning

confidence: 99%

Direct evidence of ZnO morphology modification via the selective adsorption of ZnO-binding peptides

et al. 2011

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Biomolecule-mediated ZnO synthesis has great potential for the tailoring of ZnO morphology for specific application in biosensors, window materials for display and solar cells, dye-sensitized solar cells (DSSCs), biomedical materials, and photocatalysts due to its specificity and multi-functionality. In this contribution, the effect of a ZnO-binding peptide (ZnO-BP, G-12: GLHVMHKVAPPR) and its GGGC-tagged derivative (GT-16: GLHVMHKVAPPRGGGC) on the growth of ZnO crystals expressing morphologies dependent on the relative growth rates of (0001) and (10 10) planes of ZnO have been studied. The amount of peptide adsorbed was determined by a depletion method using oriented ZnO films grown by Atomic Layer Deposition (ALD), while the adsorption behavior of G-12 and GT-16 was investigated using XPS and a computational approach. Direct evidence was obtained to show that (i) both the ZnO-BP identified by phage display and its GGGC derivative (GT-16) are able to bind to ZnO and modify crystal growth in a molecule and concentration dependent fashion, (ii) plane selectivity for interaction with the (0001) versus the (10 10) crystal planes is greater for GT-16 than G-12; and (iii) specific peptide residues interact with the crystal surface albeit in the presence of charge compensating anions. To our knowledge, this is the first study to provide unambiguous and direct quantitative experimental evidence of the modification of ZnO morphology via (selective and nonselective) adsorption-growth inhibition mechanisms mediated by a ZnO-BP identified from phage display libraries.

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Selection and characteristics of peptides that bind thermally grown silicon dioxide films

Cited by 55 publications

References 17 publications

A Dimeric Peptide That Binds Selectively to Prostate-Specific Membrane Antigen and Inhibits its Enzymatic Activity

A Dimeric Peptide That Binds Selectively to Prostate-Specific Membrane Antigen and Inhibits its Enzymatic Activity

Molecular biomimetics: nanotechnology and bionanotechnology using genetically engineered peptides

Direct evidence of ZnO morphology modification via the selective adsorption of ZnO-binding peptides

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