Smart drug delivery against Helicobacter pylori: pectin-coated, mucoadhesive liposomes with antiadhesive activity and antibiotic cargo

The first step in the development of Helicobacter pylori pathogenicity is the receptor-mediated adhesion to the gastric epithelium. Inhibition of outer membrane proteins of H . pylori (e.g. BabA) by antiadhesive drugs will contribute to reduced recolonization and infection. Pectin from apple inhibit...

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Bibliographic Details
Published in:	Applied microbiology and biotechnology Vol. 104; no. 13; pp. 5943 - 5957
Main Authors:	Gottesmann, Maren, Goycoolea, Francisco M., Steinbacher, Tim, Menogni, Tamara, Hensel, Andreas
Format:	Journal Article
Language:	English
Published:	Berlin/Heidelberg Springer Berlin Heidelberg 01-07-2020 Springer Springer Nature B.V
Subjects:	3-Aminobutyric acid Adhesins, Bacterial - metabolism Adhesion Amoxicillin Amoxicillin - chemistry Amoxicillin - pharmacology Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Antibiotics Applied Microbial and Cell Physiology Bacterial Adhesion - drug effects Biomedical and Life Sciences Biotechnology Cargo Cell Line Coating Coatings Confocal microscopy Cytotoxicity Drug carriers Drug delivery Drug Delivery Systems Drugs Encapsulation Epithelial cells Epithelium Gastric Mucins - metabolism Gastric Mucosa - metabolism Gastric Mucosa - microbiology Health aspects Helicobacter pylori Helicobacter pylori - drug effects Helicobacter pylori - metabolism Humans Infection Infection control Life Sciences Lipopolysaccharides - metabolism Liposomes Liposomes - chemistry Liposomes - metabolism Membrane proteins Microbial Genetics and Genomics Microbiology Mucin Mucins Mucus Outer membrane proteins Pathogenicity Pathogens Pectin Pectins - chemistry Polydispersity Recolonization Scanning microscopy Smart drugs and nutrients Stomach Swine Toxicity Vehicles Zeta potential Germany Bacterial antiadhesion Pectin Liposomes Mucoadhesion Adhesion Helicobacter pylori
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Summary:	The first step in the development of Helicobacter pylori pathogenicity is the receptor-mediated adhesion to the gastric epithelium. Inhibition of outer membrane proteins of H . pylori (e.g. BabA) by antiadhesive drugs will contribute to reduced recolonization and infection. Pectin from apple inhibits the BabA and LPS-mediated adhesion of H . pylori to human stomach cells. Pectin-coated liposomes with encapsulated amoxicillin were characterized for polydispersity, zeta potential, encapsulation efficiency, stability, and amoxicillin release. Coated liposomes did not influence the viability of AGS and HT29-MTX cells up to 100 μg/mL but exert cytotoxicity against H . pylori at 10 μg/mL. Pectin-coating of liposomes provoked direct interaction and subsequent binding of the particles to surface structures of H . pylori , and interaction with mucus from porcine stomach and mucus secreted by HT29-MTX cells. Laser scanning microscopy of H . pylori and AGS cells together with liposomes indicated co-aggregation. The mucoadhesive effect seems interesting as stomach cells are covered by a mucus layer. H . pylori is able to penetrate and cross the mucin rapidly to reach pH-neutral epithelium to escape the acidic environment, followed by interaction with epithelial cells. In summary, all experimental evidence is consistent with a specific interaction of pectin-coated liposomes with mucins and surface structures of H . pylori . As the coated liposomes show mucoadhesion to the negatively charged mucins, docking to stomach mucin, mucus penetration, and recognition of and adhesion to H . pylori , they can be considered a novel type of multifunctional drug carriers for local antibiotic therapy against H . pylori . Key points • Smart, multifunctional mucoadhesive liposomes • Specific targeting against BabA/LPS of Helicobacter pylori • Inhibition of bacterial adhesion of H. pylori to human host cells • Release of antibiotic cargo
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0175-7598 1432-0614
DOI:	10.1007/s00253-020-10647-3