| Autor: |
Štimac, Adela, Frkanec, Leo, Frkanec, Ruža |
| Přispěvatelé: |
Frkanec, Leo, Namjesnik, Danijel, Tomišić, Vladislav |
| Jazyk: |
angličtina |
| Rok vydání: |
2019 |
| Předmět: |
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| Popis: |
Peptidoglycan is the major component of bacterial cell walls which is recognized by the innate immune system through a series of pattern recognition receptors (PRR), which play a key role in first-line defense of the body. Lectins, naturally occurring carbohydrate-binding proteins, are involved in numerous biological processes and some of them act as PRR and bind significantly to PGN. In this study we were primarily interested to test interaction of peptidoglycan monomer (GlcNAc- MurNac-LAla-D-isoGln-mesoDAP(εNH2)-DAla-D-Ala, PGM), disaccharide pentapeptide isolated from B. divaricatum with model plant lectin, wheat germ agglutinin (WGA), by quartz crystal microbalance (QCM) method (Figure 1). WGA has a high binding affinity for N-acetyl-glucosamine (GlcNAc), one of the essential components of PG glycan strands. In order to study interactions of PGM with lectins, lipophilic derivative, PGM-oleyl was synthesized and was used for preparation of the self-assembled hybrid bilayer membrane (HBM). The results showed that PGM was effectively recognized by WGA and that strength of interactions depend on amount of PGM-oleil used for HBM preparation. The association constant for the binding of WGA to PGM functionalized hybrid bilayers was determined. It was demonstrated that the use of functionalized self-assembled bilayer as a biosensing platform has the potential to become a powerful tool for the study of other glycans by using a greater variety of lectins. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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