Academic Journal

The assessment of Pseudomonas aeruginosa lectin LecA binding characteristics of divalent galactosides using multiple techniques

التفاصيل البيبلوغرافية
العنوان: The assessment of Pseudomonas aeruginosa lectin LecA binding characteristics of divalent galactosides using multiple techniques
المؤلفون: Zaree, Pouya, Torano, Javier Sastre, de Haan, Cornelis A M, Scheltma, Richard A, Barendregt, Arjan, Thijssen, Vito, Yu, Guangyun, Flesch, Frits, Pieters, Roland J
المساهمون: Afd Chemical Biology and Drug Discovery, Virologie, dI&I I&I-1, Afd Biomol.Mass Spect. and Proteomics, Sub Biomol.Mass Spectrometry & Proteom., Chemical Biology and Drug Discovery, Biomolecular Mass Spectrometry and Proteomics
سنة النشر: 2021
مصطلحات موضوعية: binding kinetics, LecA inhibition, multivalency, protein–carbohydrate interactions, residence time
الوصف: Pseudomonas aeruginosa is a widespread opportunistic pathogen that is capable of colonizing various human tissues and is resistant to many antibiotics. LecA is a galactose binding tetrameric lectin involved in adhesion, infection and biofilm formation. This study reports on the binding characteristics of mono- and divalent (chelating) ligands to LecA using different techniques. These techniques include Affinity Capillary Electrophoresis (ACE), Bio Layer Interferometry (BLI), Native Mass Spectrometry and a Thermal Shift Assay. Aspects of focus include: affinity, selectivity, binding kinetics and residence time. The affinity of a divalent ligand was determined to be in the low nanomolar range for all of the used techniques and with a ligand residence time of approximately 7 hours, while no strong binding was seen to related lectin tetramers. Each of the used techniques provides a unique and complementary insight into the chelation based binding mode of the divalent ligand to the LecA tetramer.
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
تدمد: 0959-6658
Relation: https://dspace.library.uu.nl/handle/1874/412720
الاتاحة: https://dspace.library.uu.nl/handle/1874/412720
Rights: info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.9959F95E
قاعدة البيانات: BASE