| Literature DB >> 29399607 |
Edikan Archibong1, Alexander Foster2, Keirsten Caldwell2, Adrian Lita3, Bereket Mochona2, Nelly Mateeva2.
Abstract
Aniline-peptide (FLDQV, FLDQVC, Dansyl-FLDQV, Dansyl-FLDQVC, and FLDQV-AMC) mixtures underwent oxidative chemical and electrochemical polymerization in excess of aniline. The products of the chemical polymerization were low molecular weight polymers containing more than 70% peptide. Electrochemically polymerized species polyaniline-FLDQV (PANI-FLDQV) consisted mainly of polyaniline units containing about 10% peptide. The solubility of the latter in 1,1,1,3,3,3-hexafluoro-2-propanol (HFP) was similar to the camphorsulfonic acid (CSA) doped emeraldine base (PANI-CSA) solubility, however the weight composition of the electrospun fibers produced from the two polymers was significantly different. 2D 1H-13C HSQC analyses were employed to analyze the binding between the aniline and peptide moieties. Binding of peptide to polyaniline is reflected by the appearance of extra cross-peaks which display line broadening between the free polyaniline and the free pentapeptide. Peptides may be chemically bonded to the polymer molecules, but they may also act as doping agents to the nitrogen atoms via hydrogen bonding.Entities:
Keywords: Electrospinning; Peptides; Polyaniline; Polymerization
Year: 2016 PMID: 29399607 PMCID: PMC5794223 DOI: 10.1016/j.apmt.2016.07.004
Source DB: PubMed Journal: Appl Mater Today ISSN: 2352-9407