Accession Number : ADA617452


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


Descriptive Note : Journal article


Corporate Author : MICHIGAN UNIV ANN ARBOR


Personal Author(s) : Han, Xiaofeng ; Uzarski, Joshua R ; Mello, Charlene M ; Chen, Zhan


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a617452.pdf


Report Date : 06 Aug 2013


Pagination or Media Count : 11


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.


Descriptors :   *ORIENTATION(DIRECTION) , *PEPTIDES , EXPERIMENTAL DESIGN , MOLECULAR STRUCTURE , SPECTROSCOPY


Subject Categories : Biochemistry
      Genetic Engineering and Molecular Biology
      Physical Chemistry


Distribution Statement : APPROVED FOR PUBLIC RELEASE