Publications by authors named "L E Preuss"

Article Synopsis
  • - Biofilms can resist traditional antibiotics, prompting the search for new antimicrobials from unique sources like aquatic microorganisms, leading to the analysis of microalgae-bacteria communities for potential antimicrobial enzymes.
  • - A promising enzyme candidate called Dlh3 was found to inhibit biofilm development of the fish pathogen Edwardsiella anguillarum by up to 54.5% and showed positive effects on self-defense genes in response to its application.
  • - Dlh3 demonstrates biotechnological potential for aquaculture because it effectively inhibits harmful biofilms without negatively affecting the health or growth of a relevant fish cell model (CHSE-214).
View Article and Find Full Text PDF

The use of surface-grafted polymer brushes with combined low-fouling and antibacterial functionality is an attractive strategy to fight biofilm formation. This report describes a new styrene derivative combining a quaternary ammonium group with a sulfobetaine group in one monomer. Surface-initiated polymerization of this monomer on titanium and a polyethylene (PE) base material gave bifunctional polymer brush layers.

View Article and Find Full Text PDF

Aims: Pressure overload (PO) and volume overload (VO) lead to concentric or eccentric hypertrophy. Previously, we could show that activation of signalling cascades differ in in vivo mouse models. Activation of these signal cascades could either be induced by intrinsic load sensing or neuro-endocrine substances like catecholamines or the renin-angiotensin-aldosterone system.

View Article and Find Full Text PDF

Certain members of the Actinobacteria and Proteobacteria are known to degrade polyethylene terephthalate (PET). Here, we describe the first functional PET-active enzymes from the Bacteroidetes phylum. Using a PETase-specific Hidden-Markov-Model- (HMM-) based search algorithm, we identified several PETase candidates from Flavobacteriaceae and Porphyromonadaceae.

View Article and Find Full Text PDF

The capsid of human papillomavirus (HPV) consists of two capsid proteins - the major capsid protein L1 and the minor capsid protein L2. Assembled virus-like particles, which only consist of L1 proteins, are successfully applied as prophylactic vaccines against HPV infections. The capsid subunits are L1-pentamers, which are also reported to protect efficiently against HPV infections in animals.

View Article and Find Full Text PDF