Adsorption Behavior of Linear and Cyclic Genetically Engineered Platinum Binding Peptides

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• 作者：Urartu Ozgur Safak Seker ; Brandon Wilson ; Sevil Dincer ; Il Won Kim ; Ersin Emre Oren ; John Spencer Evans ; Candan Tamerler ; Mehmet Sarikaya
• 刊名：Langmuir
• 出版年：2007
• 出版时间：July 17, 2007
• 年：2007
• 卷：23
• 期：15
• 页码：7895 - 7900
• 全文大小：417K
• 年卷期：v.23,no.15(July 17, 2007)
• ISSN：1520-5827

文摘

Recently, phage and cell-surface display libraries have been adapted for genetically selecting short peptides for avariety of inorganic materials. Despite the enormous number of inorganic-binding peptides reported and theirbionanotechnological utility as synthesizers and molecular linkers, there is still a limited understanding of molecularmechanisms of peptide recognition of and binding to solid materials. As part of our goal of genetically designing thesepeptides, understanding the binding kinetics and thermodynamics, and using the peptides as molecular erectors, inthis report we discuss molecular structural constraints imposed upon the quantitative binding characteristics of peptideswith an affinity for inorganics. Specifically, we use a high-affinity seven amino acid Pt-binding sequence, PTSTGQA,as we reported in earlier studies and build two constructs: one is a Cys-Cys constrained "loop" sequence (CPTSTGQAC)that mimics the domain used in the pIII tail sequence of the phage library construction, and the second is the linearform, a septapeptide, without the loop. Both sequences were analyzed for their adsorption behavior on Pt thin filmsby surface plasmon resonance (SPR) spectroscopy and for their conformational properties by circular dichroism (CD).We find that the cyclic peptide of the integral Pt-binding sequence possesses single or 1:1 Langmuir adsorptionbehavior and displays equilibrium and adsorption rate constants that are significantly larger than those obtained forthe linear form. Conversely, the linear form exhibits biexponential Langmuir isotherm behavior with slower andweaker binding. Furthermore, the structure of the cyclic version was found to adopt a random coil molecular conformation,whereas the linear version adopts a polyproline type II conformation in equilibrium with the random coil. The 2,2,2-trifluoroethanol titration experiments indicate that TFE has a different effect on the secondary structures of the linearand cyclic versions of the Pt binding sequence. We conclude that the presence of the Cys-Cys restraint affects boththe conformation and binding behavior of the integral Pt-binding septapeptide sequence and that the presence orabsence of constraints could be used to tune the adsorption and structural features of inorganic binding peptidesequences.