Dynamic force spectroscopy of the specific interaction between the PDZ domain and its recognition peptides

Tei Maki, Satoru Kidoaki, Kengo Usui, Harukazu Suzuki, Masayoshi Ito, Fuyu Ito, Yoshihide Hayashizaki, Takehisa Matsuda

Research output: Contribution to journalArticle

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Abstract

To characterize the molecular basis of specific interactions of PDZ proteins, dynamic force spectroscopy (DFS) for the PDZ protein Tax-interacting protein-1 (TIP-1) and its recognition peptide (PDZ-pep) derived from β-catenin was performed using an atomic force microscope (AFM), together with measurement of thermodynamic and kinetic parameters using surface plasmon resonance (SPR). The unbinding force of this pair was measured under different conditions of AFM tip-retraction velocity. The relationship between the unbinding force and the logarithmic force-loading rate, that is, the dynamic force spectrum, exhibited two different rate regimes, for each of which the forces increased linearly with the force-loading rate. On the basis of the theoretical treatment of the Bell-Evans model, the positions of two different activation barriers in the reaction coordinate and dissociation rate constants in each barrier were evaluated from slopes and x-intercepts of the two linear regimes (first barrier: 0.04 nm and 1.10 × 10s-1; second barrier: 0.21 nm and 2.77 × 10-2 s-1, respectively). Although two-step unbinding kinetics between TIP-1 and PDZ-pep was suggested from the DFS analysis, SPR results showed single-step dissociation kinetics with a rate constant of 2.89 × 10-1 s-1. Different shapes of the free energy profile of the unbinding process were deduced from each result of DFS and SPR. The reason for such topographic differences in the energy landscape is discussed in relation to the differences in the pathways of forced unbinding and spontaneous dissociation.

Original languageEnglish
Pages (from-to)2668-2673
Number of pages6
JournalLangmuir
Volume23
Issue number5
DOIs
Publication statusPublished - Feb 27 2007

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Peptides
peptides
Surface plasmon resonance
Spectroscopy
Proteins
Taxation
spectroscopy
Rate constants
Microscopes
tax Gene Products
interactions
Catenins
Kinetics
surface plasmon resonance
Kinetic parameters
proteins
Free energy
loading rate
dissociation
Chemical activation

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

Cite this

Dynamic force spectroscopy of the specific interaction between the PDZ domain and its recognition peptides. / Maki, Tei; Kidoaki, Satoru; Usui, Kengo; Suzuki, Harukazu; Ito, Masayoshi; Ito, Fuyu; Hayashizaki, Yoshihide; Matsuda, Takehisa.

In: Langmuir, Vol. 23, No. 5, 27.02.2007, p. 2668-2673.

Research output: Contribution to journalArticle

Maki, T, Kidoaki, S, Usui, K, Suzuki, H, Ito, M, Ito, F, Hayashizaki, Y & Matsuda, T 2007, 'Dynamic force spectroscopy of the specific interaction between the PDZ domain and its recognition peptides', Langmuir, vol. 23, no. 5, pp. 2668-2673. https://doi.org/10.1021/la0627011
Maki, Tei ; Kidoaki, Satoru ; Usui, Kengo ; Suzuki, Harukazu ; Ito, Masayoshi ; Ito, Fuyu ; Hayashizaki, Yoshihide ; Matsuda, Takehisa. / Dynamic force spectroscopy of the specific interaction between the PDZ domain and its recognition peptides. In: Langmuir. 2007 ; Vol. 23, No. 5. pp. 2668-2673.
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