Different Interfacial Behaviors of N- and C-Terminus Cysteine-Modified Cecropin P1 Chemically Immobilized onto Polymer Surface

Abstract

Sum frequency generation (SFG) vibrational spectroscopy and attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) were used to investigate the orientation of N-terminus cysteine-modified cecropin P1 (cCP1) at the polystyrene maleimide (PS-MA)/ peptide phosphate buffer solution interface. The cCP1 cysteine group reacts with the maleimide group on the PS-MA surface to chemically immobilize cCP1. Previously, we found that the C-terminus cysteine-modified cecropin P1 (CP1c) molecules exhibit a multiple-orientation distribution at the PS-MA/peptide phosphate buffer solution interface, due to simultaneous physical adsorption and chemical immobilization of CP1c on the PS-MA surface. Differently, in this research, it was found that the interfacial orientation of cCP1 molecules varied from a horizontal orientation to the tilting orientation to the standing up orientation and then to the multiple-orientation distribution as the peptide concentration increased from 0.19 to 3.74 microM. This research shows the different interaction mechanisms between CP1c and PS-MA and between cCP1 and PS-MA.

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Document Details

Document Type
Technical Report
Publication Date
Aug 06, 2013
Accession Number
ADA617452

Entities

People

  • Charlene M. Mello
  • Joshua R Uzarski
  • Xiaofeng Han
  • Zhan Chen

Organizations

  • University of Michigan

Tags

Communities of Interest

  • Sensors

DTIC Thesaurus Topics

  • Buffers (Chemistry)
  • Chemical Synthesis
  • Chemistry
  • Detection
  • Dielectric Polymers
  • Films
  • Gaussian Distributions
  • Molecular Dynamics
  • Molecules
  • Orientation (Direction)
  • Pathogenic Bacteria
  • Polymeric Films
  • Polymers
  • Self Assembled Monolayers
  • Spectra
  • Spectroscopy
  • United States

Readers

  • Molecular and Cellular Biochemistry
  • Polymer Science and Technology