Thermodynamics of Engineered Gold Binding Peptides: Establishing the Structure-Activity Relationships


Seker U. O. S. , Wilson B., Kulp J. L. , Evans J. S. , Tamerler C., Sarikaya M.

BIOMACROMOLECULES, cilt.15, sa.7, ss.2369-2377, 2014 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 15 Konu: 7
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1021/bm4019006
  • Dergi Adı: BIOMACROMOLECULES
  • Sayfa Sayıları: ss.2369-2377

Özet

Adsorption behavior of a gold binding peptide was experimentally studied to achieve kinetics and thermodynamics parameters toward understanding of the binding of an engineered peptide onto a solid metal surface. The gold-binding peptide, GBP1, was originally selected using a cell surface display library and contains 14 amino acid residues. In this work, single- and three-repeats of GBP1 were used to assess the effects of two parameters: molecular architecture versus secondary structure on adsorption on to gold substrate. The adsorption measurements were carried out using surface plasmon resonance (SPR) spectroscopy at temperatures ranging from 10 to 55 degrees C. At all temperatures, two different regimes of peptide adsorption were observed, which, based on the model, correspond to two sets of thermodynamics values. The values of enthalpy, Delta H-ads, and entropy, Delta S-ads, in these two regimes were determined using the van't Hoff approach and Gibbs-Helmholtz relationship. In general, the values of enthalpy for both peptides are negative indicating GBP1 binding to gold is an exothermic phenomenon and that the binding of three repeat gold binding peptide (31-GBP1) is almost S times tighter than that for the single repeat (1-GBP1). More intriguing result is that the entropy of adsorption for the 3l-GBP1 is negative (-43.4 +/- 8.5 cal/(mol K)), while that for the 1-GBP1 is positive (10.90 +/- 1.3 cal/(mol K)). Among a number of factors that synergistically contribute to the decrease of entropy, long-range ordered self-assembly of the 31-GBP1 on gold surface is the most effective, probably through both peptide solid and peptide peptide intermolecular interactions. Additional adsorption experiments were conducted in the presence of 2,2,2-trifluoroethanol (TFE) to determine how the conformational structures of the biomolecules responded to the environmental perturbation. We found that the peptides differ in their conformational responses to the change in solution conditions; while 1-GBP does not fold in the presence of TFE, 31-GBP1 adopted two types of secondary structure (beta-strand, alpha-helix) and that peptide's binding to the solid is enhanced by the presence of low percentages of TFE solvent. Not only do these kinetics and thermodynamics results provide adsorption behavior and binding of genetically engineered peptides for inorganics (GEPI), but they could also provide considerable insights into fundamental understanding peptide molecular recognition and their selective specificity for the solids. Moreover, comprehensive work described herein suggests that multiple repeat forms of the solid binding peptides possess a conformational component that can be exploited to further tailor affinity and binding of a given sequence to a solid material followed by ordered assembly as a convenient tool in future practical applications.