Title
Orientation Determination of a Hybrid Peptide Immobilized on CVD-Based Reactive Polymer Surfaces
Author
Shuai Wei, Xingquan Zou, Kenneth Cheng, Joshua Jasensky, Qiuming Wang, Yaoxin Li, Joerg Lahann, Charles L. Brooks, Zhan Chen
Year
2016
Journal
The Journal of Physical Chemistry C
Abstract
Antimicrobial peptides (AMPs), due to their unique structure/function relationship, have great potential to be developed into novel diagnostic and therapeutic agents for a variety of pathogens and illnesses. Often such peptides are administered using powder or suspension, limiting their reusability or recyclability. Immobilization of these antimicrobial peptides on biotic/abiotic surfaces may circumvent such disadvantages, but the immobilization is likely to not only change the peptide secondary structures and orientations, but also ultimately affect the functionality of such peptides. In order to better understand surface-bound structures of AMPs on abiotic surfaces, cecropin A (1-8)-melittin (1-18) hybrid peptides were chemically immobilized on polymer surfaces prepared by chemical vapor deposition (CVD) polymerization. Measurements by sum frequency generation (SFG) vibrational spectroscopy and circular dichroism were used to characterize the peptides immobilized on the CVD-based polymer in situ. In addition, coarse-grained molecular dynamics (MD) simulations were used to understand the hybrid peptide orientations on the molecular level. Simulation results were highly consistent with the experimental data. Results indicated that, unlike other linear peptides immobilized on similar abiotic surfaces, this hybrid peptide immobilized on CVD-based polymer surfaces exhibited two bending points. Such conclusions help further understand the role surface immobilization has on such unique molecules.
Instrument
J-1500
Keywords
Circular dichroism, Secondary structure, Polymers, Biochemistry