posted on 2021-10-19, 05:13authored byCindy
D. Beyer, Sugina Thavalingam, Tatiana Guseva, Lisa Schardt, Ralf Zimmermann, Carsten Werner, Pascal Dietze, Julia Elisabeth Bandow, Nils Metzler-Nolte, Axel Rosenhahn
Zwitterionic peptides
are facile low-fouling compounds for environmental
applications as they are biocompatible and fully biodegradable as
their degradation products are just amino acids. Here, a set of histidine
(H) and glutamic acid (E), as well as lysine (K) and glutamic acid
(E) based peptide sequences with zwitterionic properties were synthesized.
Both oligopeptides (KE)4K and (HE)4H were synthesized
in d and l configurations to test their ability
to resist the nonspecific adsorption of the proteins lysozyme and
fibrinogen. The coatings were additionally tested against the attachment
of the marine organisms Navicula perminuta and Cobetia marina as well as the freshwater bacterium Pseudomonas fluorescens on the developed coatings. While
the peptides containing lysine performed better in protein resistance
assays and against freshwater bacteria, the sequences containing histidine
were generally more resistant against marine organisms. The contribution
of amino acid-intrinsic properties such as side chain pKa values and hydrophobicity, as well as external parameters
such as pH and salinity of fresh water and seawater on the resistance
of the coatings is discussed. In this way, a detailed picture emerges
as to which zwitterionic sequences show advantages in future generations
of biocompatible, sustainable, and nontoxic fouling release coatings.