Sandbox 127: Difference between revisions

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== PBP2a and Ceftobiprole ==
== B-Lactams that Inhibit PBP2a==


MRSA becomes resistant to β-lactams by acquiring an alternative PBP, PBP2a, that is
MRSA becomes resistant to almost all β-lactams by acquiring an alternative TP, PBP2a, that is
neither bound nor inhibited by β-lactams. Recently, two cephalosporins –  
neither bound nor inhibited by β-lactams. Recently, two cephalosporins –  
<scene name='37/372724/Medicine_interaction/4'>cefobiprole</scene> and
<scene name='37/372724/Medicine_interaction/4'>cefobiprole</scene> and
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inhibit PBP2a because additional chemical groups at the  
inhibit PBP2a because additional chemical groups at the  
<scene name='37/372724/Medicine_interaction/3'>R2</scene>
<scene name='37/372724/Medicine_interaction/3'>R2</scene>
position of the cephalosporin backbone are able to interact with additional amino acid
position of the ceftobiprole are able to interact with additional amino acid
residues in PBP2a; specifically  
residues in PBP2a; specifically  
<scene name='37/372724/Medicine_interaction/2'>Tyr446 and Met641</scene>. The
<scene name='37/372724/Medicine_interaction/2'>Tyr446 and Met641, and increase the association of ceftobiprole with PBP2a</scene>. As such, ceftobiprole is (shown as colors of the atom types ([[CPK]]))is able to more efficiently react with <scene name='37/372724/R2_interaction/9'>Ser403</scene> and therefore inhibit the activity of PBP2a.
<scene name='37/372724/Medicine_interaction/1'> medicine</scene> shown as colors of the atom types ([[CPK]]) is able to more efficiently react with <scene name='37/372724/R2_interaction/9'>Ser403</scene> and therefore inhibit the activity of PBP2a as a result of ceftobiprole <scene name='37/372724/R2_interaction/8'>tighter binding</scene> to PBP2a. Unlike penicillin, this results in inhibition of PBP2a.