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Partitioning the Loss in Vancomycin Binding Affinity for <scp>d</scp>-Ala-<scp>d</scp>-Lac into Lost H-Bond and Repulsive Lone Pair Contributions
- Source :
- Journal of the American Chemical Society. 125:9314-9315
- Publication Year :
- 2003
- Publisher :
- American Chemical Society (ACS), 2003.
-
Abstract
- The binding affinity of 4, which incorporates a methylene (CH2) in place of the key linking amide of Ac2-l-Lys-d-Ala-d-Ala, for vancomycin was compared with that of Ac2-l-Lys-d-Ala-d-Ala (3) and Ac2-l-Lys-d-Ala-d-Lac (5). The vancomycin affinity for 4 was approximately 10-fold less than that of 3, but 100-fold greater than that of 5. This suggests that the reduced binding affinity of 5 (4.1 kcal/mol) may be attributed to both the loss of a key H-bond (1.5 kcal/mol) and a destabilizing lone pair/lone pair electrostatic interaction introduced with the ester oxygen of 5 (2.6 kcal/mol) with the latter, not the H-bond, being responsible for the largest share of the 1000-fold reduction.
- Subjects :
- chemistry.chemical_classification
Chemistry
Stereochemistry
Hydrogen bond
Hydrogen Bonding
Peptide
Dipeptides
General Chemistry
Biochemistry
Catalysis
Anti-Bacterial Agents
Kinetics
chemistry.chemical_compound
Colloid and Surface Chemistry
Vancomycin
Amide
Mole
Lactates
Thermodynamics
Methylene
Oligopeptides
Lone pair
Antibacterial agent
Electrostatic interaction
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 125
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....1ad63f720f6a966bba9260376d6b7439