Structure-Based Design Approaches to Cell Wall Biosynthesis Inhibitors
This review summarizes some of the published attempts to incorporate protein and NMR structures in the design of new antibiotics that specifically target Cell Wall biosynthesis. Most of the steps involved in peptidglycan synthesis have been investigated as potential strategies against cell wall inhi...
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Published in | Current pharmaceutical design Vol. 9; no. 11; pp. 857 - 866 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United Arab Emirates
Bentham Science Publishers Ltd
01.01.2003
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Subjects | |
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Abstract | This review summarizes some of the published attempts to incorporate protein and NMR structures in the design of new antibiotics that specifically target Cell Wall biosynthesis. Most of the steps involved in peptidglycan synthesis have been investigated as potential strategies against cell wall inhibition. Structural information has been most useful in the design of molecules in the Mur enzyme pathway, penicillin binding proteins and lactamases, as well as proteins that are part of the final steps of transglycosylation - in particular, d-Ala-d-Ala ligase. Several unique issues exist in the design of effective antibacterials, such as the significant differences in protein structure between organisms, such as the case of MurB in which a large amino acid loop that occupies the active site of the E. Coli is gone in the Staph aureus enzyme. Additionally, bacterial resistance is an important issue, and in some cases, structural information can be used to understand the source of this resistance. For example, mutations within the d-Ala-d-Ala ligases lead to the inability of Vancomycin antibiotics to bind. |
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AbstractList | This review summarizes some of the published attempts to incorporate protein and NMR structures in the design of new antibiotics that specifically target Cell Wall biosynthesis. Most of the steps involved in peptidglycan synthesis have been investigated as potential strategies against cell wall inhibition. Structural information has been most useful in the design of molecules in the Mur enzyme pathway, penicillin binding proteins and lactamases, as well as proteins that are part of the final steps of transglycosylation - in particular, d-Ala-d-Ala ligase. Several unique issues exist in the design of effective antibacterials, such as the significant differences in protein structure between organisms, such as the case of MurB in which a large amino acid loop that occupies the active site of the E. Coli is gone in the Staph aureus enzyme. Additionally, bacterial resistance is an important issue, and in some cases, structural information can be used to understand the source of this resistance. For example, mutations within the d-Ala-d-Ala ligases lead to the inability of Vancomycin antibiotics to bind. |
Author | Alan Katz Craig Caufield |
Author_xml | – sequence: 1 givenname: Alan H surname: Katz fullname: Katz, Alan H email: KATZA@wyeth.com organization: Wyeth-Ayerst Research, Princeton, NJ 08540, USA. KATZA@wyeth.com – sequence: 2 givenname: Craig E surname: Caufield fullname: Caufield, Craig E |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12678870$$D View this record in MEDLINE/PubMed |
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SubjectTerms | Alkyl and Aryl Transferases - antagonists & inhibitors Anti-Bacterial Agents Anti-Infective Agents - pharmacology Bacteria - drug effects Bacteria - enzymology Bacterial Proteins Carrier Proteins - antagonists & inhibitors Cell Wall - drug effects Cell Wall - enzymology Drug Design Fungi - drug effects Fungi - enzymology Hexosyltransferases Muramoylpentapeptide Carboxypeptidase - antagonists & inhibitors Penicillin-Binding Proteins Peptidoglycan - biosynthesis Peptidyl Transferases Structure-Activity Relationship |
Title | Structure-Based Design Approaches to Cell Wall Biosynthesis Inhibitors |
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