Studies of mutant lectin binding behaviour by microcalorimetry

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F14%3A00077914" target="_blank" >RIV/00216224:14310/14:00077914 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Studies of mutant lectin binding behaviour by microcalorimetry
Original language description
Bacterial lectins help pathogens in adhesion to sugar moieties presented on the host cell surface. Therefore, lectins from pathogenic bacteria and their adhesion modes are the subject of intense study. On the other hand, understanding of the basic principles of the lectin-carbohydrate binding process is still important task and can be helpful for further lectin engineering by targeted mutagenesis methods. Lectins with tuned affinity can offer interesting perspectives in biomedical or biotechnology. Ourwork is focused on the engineering of previously well studied lectins PA-IIL [1], CV-IIL [2], RS-IIL [3] and BC2L-A [4] from the PA-IIL lectin family. Effects of the mutations on the individual lectin binding behaviour were studied by isothermal titration microcalorimetry method (ITC).
Czech name
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Czech description
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Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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