Conformational analysis of β and γ-lactam antibiotics
✍ Scribed by J Lamotte; G Dive; JM Ghuysen
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- French
- Weight
- 709 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0223-5234
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Conformational‐energy calculations were carried out on the new family of β‐lactam antibiotics (viz., thienamycin, PS‐5, 1‐oxa‐ and 1‐thiapenems, and their close analogs); these exhibit broad‐spectrum antibacterial activity and stability towards β‐lactamase‐producing strains. The bicycli
reevaluation of beta-lactam bond deformation as a criterion for a penicillin-like mode-of-action. ## 11. MECHANISM OF ACTION The mechanism of action of the naturally-occurring monobactams was examined at an early They were shown to interact with certain of the penicillin-binding proteins (PBP's) o
The homochiral 3-amino-1-(4-methoxyphenyl)-4-phenyl-βlactam (ϵ Alm) was conjugated with Boc-Ala to give Ala-Alm (9) after Boc deprotection (Boc = tert-butoxycarbonyl, Ala = alanine). Coupling of Fc-COOH (1) and Boc-Fca (10) with "dipeptide" 9 resulted in the formation of Fc-CO-Ala-Alm ( ) and the tr