| Literature DB >> 33540553 |
Lena Heinbockel1, Günther Weindl2, Wilmar Correa3, Julius Brandenburg4, Norbert Reiling4, Karl-Heinz Wiesmüller5, Tobias Schürholz6, Thomas Gutsmann3, Guillermo Martinez de Tejada7, Karl Mauss1,8, Klaus Brandenburg1.
Abstract
The polypeptide Pep19-2.5 (Aspidasept®) has been described to act efficiently against infection-inducing bacteria by binding and neutralizing their most potent toxins, i.e., lipopolysaccharides (LPS) and lipoproteins/peptides (LP), independent of the resistance status of the bacteria. The mode of action was described to consist of a primary Coulomb/polar interaction of the N-terminal region of Pep19-2.5 with the polar region of the toxins followed by a hydrophobic interaction of the C-terminal region of the peptide with the apolar moiety of the toxins. However, clinical development of Aspidasept as an anti-sepsis drug requires an in-depth characterization of the interaction of the peptide with the constituents of the human immune system and with other therapeutically relevant compounds such as antibiotics and non-steroidal anti-inflammatory drugs (NSAIDs). In this contribution, relevant details of primary and secondary pharmacodynamics, off-site targets, and immunogenicity are presented, proving that Pep19-2.5 may be readily applied therapeutically against the deleterious effects of a severe bacterial infection.Entities:
Keywords: Aspidasept; antimicrobial peptides; inflammation; lipopolysaccharide; pathogen-associated patterns; pharmacodynamics; sepsis
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Year: 2021 PMID: 33540553 PMCID: PMC7867136 DOI: 10.3390/ijms22031465
Source DB: PubMed Journal: Int J Mol Sci ISSN: 1422-0067 Impact factor: 5.923