Zwitterionic Peptides Reduce Accumulation of Marine and Freshwater Biofilm Formers

Beyer, C.D. and Thavalingam, S. and Guseva, T. and Schardt, L. and Zimmermann, R. and Werner, C. and Dietze, P. and Bandow, J.E. and Metzler-Nolte, N. and Rosenhahn, A.

Volume: 13 Pages: 49682-49691
DOI: 10.1021/acsami.1c13459
Published: 2021

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. © 2021 The Authors. Published by American Chemical Society.

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