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- W3036943959 abstract "Antimicrobial resistance is a growing problem in this era. Resistance to the majority of clinicalantibiotics (including those of a ‘last line of defence’ nature) has been seen in a number oflaboratory and clinical settings. One method aiming at reducing this problem is alteringexisting antimicrobial compounds, in order to improve pharmacological effects (avoidingresistance mechanisms, improved spectrum of use). Looking at the interactions between theantimicrobial compounds and their targets can determine whether modifications to currentantimicrobials (such as moenomycin A) have altered the mode of action.ecoPBP1B is a bifunctional glycosyltransferase that could be used as a model for beta lactamsand moenomycins, aiding in the design and development of novel antimicrobials based onthese families. This project aims to show whether ecoPBP1b can be used as a model for novelantimicrobials, such as seeing whether novel MoeA analogues with peptides attached (tofacilitate entry into the bacterial cell) still retain their ability to bind to glycosyltransferases.In addition, this project looked at whether different beta-lactams would significantly alterthe conformation of the transpeptidase domain of ecoPBP1b.Building on previous studies into ecoPBP1b, we managed to successfully produce usablequantities of ecoPBP1b for crystallisation in conjunction with a variety of ligands. Crystalswere produced potentially containing complexes including such compounds as AI167-p andAI168-p (MoeA analogues), cefotaxime, cephradine, and a novel beta-lactamase inhibitor(CW-019).3D structures of ecoPBP1b in complex with AI167 were produced, successfully showing theMoeA analogue bound into the transglycosylase active site. This showed that the addition ofpeptides to the moenomycin molecule has not interfered with the interactions required forthe compound to bind to the transglycosylase domain. In addition, ecoPBP1b was cocrystallised with ampicillin bound to the penicillin binding region, matching with previousstudies.There are issues that need to be addressed with regards to ecoPBP1b before it can be usedas a reliable model, especially with beta-lactams. However, the main project goal (usingecoPBP1b for novel MoeA analogues) has been achieved, as well as furthering insights intocrystallisation of proteins in general." @default.
- W3036943959 created "2020-06-25" @default.
- W3036943959 creator A5038295992 @default.
- W3036943959 date "2017-01-01" @default.
- W3036943959 modified "2023-09-27" @default.
- W3036943959 title "Investigating the Ligand Interactions Between E. coli PBP1b, Moenomycin-based Compounds, and Beta-Lactam Compounds" @default.
- W3036943959 hasPublicationYear "2017" @default.
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