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Your search keyword '"Hartmann, Laura"' showing total 21 results
Start Over Author "Hartmann, Laura" Journal biomacromolecules
21 results on '"Hartmann, Laura"'

10. Fucose-Functionalized Precision Glycomacromolecules Targeting Human Norovirus Capsid Protein

Author

Bücher, Katharina Susanne, primary, Yan, Hao, additional, Creutznacher, Robert, additional, Ruoff, Kerstin, additional, Mallagaray, Alvaro, additional, Grafmüller, Andrea, additional, Dirks, Jan Sebastian, additional, Kilic, Turgay, additional, Weickert, Sabrina, additional, Rubailo, Anna, additional, Drescher, Malte, additional, Schmidt, Stephan, additional, Hansman, Grant, additional, Peters, Thomas, additional, Uetrecht, Charlotte, additional, and Hartmann, Laura, additional

Published
2018
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14. Exploiting Oligo(amido amine) Backbones for the Multivalent Presentation of Coiled-Coil Peptides

Author

Gerling-Driessen, Ulla I. M., primary, Mujkic-Ninnemann, Nina, additional, Ponader, Daniela, additional, Schöne, Daniel, additional, Hartmann, Laura, additional, Koksch, Beate, additional, Gerling-Driessen, U. I. M., additional, Schöne, D., additional, Koksch, B., additional, Ponader, D., additional, Mujkic-Ninnemann, N., additional, and Hartmann, L., additional

Published
2015
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20. Synthesis of Homo- and Heteromultivalent Fucosylated and Sialylated Oligosaccharide Conjugates viaPreactivated N-Methyloxyamine Precision Macromolecules and Their Binding to Polyomavirus Capsid Proteins

Author

Konietzny, Patrick B., Freytag, Jasmin, Feldhof, Melina I., Müller, Joshua C., Ohl, Daniel, Stehle, Thilo, and Hartmann, Laura

Abstract

Glycoconjugates are a versatile class of bioactive molecules that have found application as vaccines and antivirals and in cancer therapy. Their synthesis typically involves elaborate functionalization and use of protecting groups on the carbohydrate component in order to ensure efficient and selective conjugation. Alternatively, non-functionalized, non-protected carbohydrates isolated from biological sources or derived through biotechnological methods can be directly conjugated via N-methyloxyamine groups. In this study, we introduce such N-methyloxyamine groups into a variety of multivalent scaffolds─from small to oligomeric to polymeric scaffolds─making use of solid-phase polymer synthesis to assemble monodisperse sequence-defined macromolecules. These scaffolds are then successfully functionalized with different types of human milk oligosaccharides deriving a library of homo- and heteromultivalent glycoconjugates. Glycomacromolecules presenting oligosaccharide side chains with either α2,3- or α2,6-linked terminal sialic acid are used in a binding study with two types of polyomavirus capsid proteins showing that the multivalent presentation through the N-methyloxyamine-derived scaffolds increases the number of contacts with the protein. Overall, a straightforward route to derive glycoconjugates from complex oligosaccharides with high variability yet control in the multivalent scaffold is presented, and applicability of the derived structures is demonstrated.

Published
2022
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21. Amphiphilic cationic β(3R3)-peptides: membrane active peptidomimetics and their potential as antimicrobial agents.

Author

Mosca S, Keller J, Azzouz N, Wagner S, Titz A, Seeberger PH, Brezesinski G, and Hartmann L

Subjects
Anti-Bacterial Agents chemical synthesis, Anti-Bacterial Agents chemistry, Cations chemical synthesis, Cations chemistry, Cations pharmacology, Cell Membrane metabolism, Dose-Response Relationship, Drug, Escherichia coli drug effects, Microbial Sensitivity Tests, Micrococcus luteus drug effects, Molecular Structure, Peptides chemical synthesis, Peptides chemistry, Pseudomonas aeruginosa drug effects, Staphylococcus aureus drug effects, Structure-Activity Relationship, Surface-Active Agents chemical synthesis, Surface-Active Agents chemistry, Anti-Bacterial Agents pharmacology, Cell Membrane drug effects, Peptides pharmacology, Peptidomimetics, Surface-Active Agents pharmacology
Abstract

We introduce a novel class of membrane active peptidomimetics, the amphiphilic cationic β(3R3)-peptides, and evaluate their potential as antimicrobial agents. The design criteria, the building block and oligomer synthesis as well as a detailed structure-activity relationship (SAR) study are reported. Specifically, infrared reflection absorption spectroscopy (IRRAS) was employed to investigate structural features of amphiphilic cationic β(3R3)-peptide sequences at the hydrophobic/hydrophilic air/liquid interface. Furthermore, Langmuir monolayers of anionic and zwitterionic phospholipids have been used to model the interactions of amphiphilic cationic β(3R3)-peptides with prokaryotic and eukaryotic cellular membranes in order to predict their membrane selectivity and elucidate their mechanism of action. Lastly, antimicrobial activity was tested against Gram-positive M. luteus and S. aureus as well as against Gram-negative E. coli and P. aeruginosa bacteria along with testing hemolytic activity and cytotoxicity. We found that amphiphilic cationic β(3R3)-peptide sequences combine high and selective antimicrobial activity with exceptionally low cytotoxicity in comparison to values reported in the literature. Overall, this study provides further insights into the SAR of antimicrobial peptides and peptidomimetics and indicates that amphiphilic cationic β(3R3)-peptides are strong candidates for further development as antimicrobial agents with high therapeutic index.

Published
2014
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