Universität zu Köln

Wenske, Sebastian, Lackmann, Jan-Wilm, Bekeschus, Sander, Weltmann, Klaus-Dieter, von Woedtke, Thomas and Wende, Kristian ORCID: 0000-0001-5217-0683 (2020). Nonenzymatic post-translational modifications in peptides by cold plasma-derived reactive oxygen and nitrogen species. Biointerphases, 15 (6). MELVILLE: AMER INST PHYSICS. ISSN 1559-4106

Full text not available from this repository.

Abstract

Cold physical plasmas are emerging tools for wound care and cancer control that deliver reactive oxygen species (ROS) and nitrogen species (RNS). Alongside direct effects on cellular signaling processes, covalent modification of biomolecules may contribute to the observed physiological consequences. The potential of ROS/RNS generated by two different plasma sources (kINPen and COST-Jet) to introduce post-translational modifications (PTMs) in the peptides angiotensin and bradykinin was explored. While the peptide backbone was kept intact, a significant introduction of oxidative PTMs was observed. The modifications cluster at aromatic (tyrosine, histidine, and phenylalanine) and neutral amino acids (isoleucine and proline) with the introduction of one, two, or three oxygen atoms, ring cleavages of histidine and tryptophan, and nitration/nitrosylation predominantly observed. Alkaline and acidic amino acid (arginine and aspartic acid) residues showed a high resilience, indicating that local charges and the chemical environment at large modulate the attack of the electron-rich ROS/RNS. Previously published simulations, which include only OH radicals as ROS, do not match the experimental results in full, suggesting the contribution of other short-lived species, i.e., atomic oxygen, singlet oxygen, and peroxynitrite. The observed PTMs are relevant for the biological activity of peptides and proteins, changing polarity, folding, and function. In conclusion, it can be assumed that an introduction of covalent oxidative modifications at the amino acid chain level occurs during a plasma treatment. The introduced changes, in part, mimic naturally occurring patterns that can be interpreted by the cell, and subsequently, these PTMs allow for prolonged secondary effects on cell physiology.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Wenske, Sebastian UNSPECIFIED UNSPECIFIED UNSPECIFIED Lackmann, Jan-Wilm UNSPECIFIED UNSPECIFIED UNSPECIFIED Bekeschus, Sander UNSPECIFIED UNSPECIFIED UNSPECIFIED Weltmann, Klaus-Dieter UNSPECIFIED UNSPECIFIED UNSPECIFIED von Woedtke, Thomas UNSPECIFIED UNSPECIFIED UNSPECIFIED Wende, Kristian UNSPECIFIED orcid.org/0000-0001-5217-0683 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-313165
DOI:	10.1116/6.0000529
Journal or Publication Title:	Biointerphases
Volume:	15
Number:	6
Date:	2020
Publisher:	AMER INST PHYSICS
Place of Publication:	MELVILLE
ISSN:	1559-4106
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language ATMOSPHERIC-PRESSURE PLASMA; PROTEIN OXIDATION; SINGLET OXYGEN; AMINO-ACIDS; IDENTIFICATION; CHEMISTRY; JET; DECONTAMINATION; QUANTIFICATION; INACTIVATION Multiple languages Biophysics; Materials Science, Biomaterials Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/31316