Orientation Determination of a Hybrid Peptide Immobilized on CVD-Based Reactive Polymer Surfaces

Autor: Joshua Jasensky, Qiuming Wang, Yaoxin Li, Kenneth Cheng, Xingquan Zou, Joerg Lahann, Shuai Wei, Zhan Chen, Christoph Hussal, Charles L. Brooks
Rok vydání: 2016
Předmět:
Zdroj: The Journal of Physical Chemistry C. 120:19078-19086
ISSN: 1932-7455
1932-7447
Popis: Antimicrobial peptides (AMPs), due to their unique structure/function relationship, have great opportunities 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 such immobilization is likely to not only change the peptide secondary structures and their orientations but also ultimately affect functionality. 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, coar...
Databáze: OpenAIRE