What is it about?
In principle, ß-lactam antibiotics bind to penicillin-binding proteins(PBPs), thereby blocking the synthesis of cell wall. However, ß-lactamases also interact with these antibiotics, cleave them and render them inactive.It is therefore interesting to highlight structural similarities and differences between, on the one hand, ß-lactamases of class A, C and D and, on the other hand, PBPs - in particular PBPs whose inactivation is lethal. This is the goal of the present work.
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Why is it important?
More specifically, the present analysis led to the detection of the residues that should be targeted by new ß-lactam antibiotics, in view of making them specific for PBP binding and avoiding ßLACT resistance in enterobacteria.
Perspectives
we can be used this result for designing novel drugs, such as new antibiotic molecules that target PBPs The approach described in this paper can be utilized as a general technique to guide in silico drug design.
Mame Ndew Mbaye
Universite de bruxelles service 3BIO-BioInfo - BioModeling, BioInformatics & BioProcesses
Read the Original
This page is a summary of: Rational antibiotic design: in silico structural comparison of the functional cavities of penicillin-binding proteins and ß-lactamases, Journal of Biomolecular Structure and Dynamics, January 2018, Taylor & Francis,
DOI: 10.1080/07391102.2017.1418678.
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