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Kamolrat Somboon. Probing binding affinities of imipenem and ertapenem with outer membrane carboxylate channel D1 (OCCD1) from P. aeruginosa : simulation studies. Master's Degree(Chemistry). Kasetsart University. Office of the University Library. : Kasetsart University, 2017.
Probing binding affinities of imipenem and ertapenem with outer membrane carboxylate channel D1 (OCCD1) from P. aeruginosa : simulation studies
Name: Kamolrat Somboon
Classification :.LCCS: RM666.A58
LCSH:
Antibiotics
LCSH:
Pseudomonas aeruginosa
Abstract:
Pseudomonas aeruginosa has been known as a notorious human pathogen. The major bottleneck to treat this infection is their substrate transport channels, which serving as the gate for nutrient and ion uptake into the cell. Normally, both general porins and substrate specific channel has been found in most gram-negative bacteria. Unfortunately, only substrate-specific channels are found in P.aeruginosa. This makes such bacteria become one of the most drug-resistance bacteria. Carbapenems are the most effective drug against P.aeruginosa. To penetrate into the cell, they employ Outer membrane carboxylate channels D1 (OccD1). In recent year, imipenem (IMI) is reported as one of the active carbapenem. In contrast, ertapenem (ERTA) shows weak activity against P. aeruginosa, even though it is in carbapem family. Understanding how each drug behaves in the recognition site of OccD1 in microscopic detail can explain why IMI is preferred over ERTA. Thus, we performed Molecular Dynamics (MD) Simulations to explore their activities inside the constriction region. Our results reveal another possible binding site in the constriction area close to the OccD1 pore. Both drugs employ lactam core part to attach themselves in the binding site and their tail to direct the passage. L132 and F133 seem to be a key for the lactam core binding. Overall, at least 4 hydrogen bonds are required in binding process. The displacement of L2 also plays an essential role. Its movement can indicate the rejection of the substrates. In IMI, L2 works with L7 to trap IMI and initiates the permeation process. For ERTA, L2 flips outwardly to allow ERTA to expose to more water and consequently get expelled. These results may lead us to improve permeability of antibiotics across bacterial outer membrane.
Kasetsart University. Office of the University Library
Address:
Bangkok
Email:
tdckulib@ku.ac.th
Name: Prapasiri Pongprayoon
Role:
Thesis Advisor
Name: Patchreenart Saparpakorn
Role:
Thesis Co-Advisor
Created:
2017
Modified:
2023-06-19
Issued:
2023-06-19
วิทยานิพนธ์/Thesis
application/pdf
URL: https://kasetsart.idm.oclc.org/login?url=https://www.lib.ku.ac.th/KUthesis/2560/kamolrat-som-all.pdf
CallNumber:
RM666.A58.K36
eng
DegreeName: Master of Science
Level: Master's Degree
Descipline: Chemistry
Grantor: Kasetsart University
©copyrights Kasetsart University
RightsAccess:
ใช้เวลา
0.032872 วินาที
Kamolrat Somboon
| Title | Contributor | Type |
|---|---|---|
| Probing binding affinities of imipenem and ertapenem with outer membrane carboxylate channel D1 (OCCD1) from P. aeruginosa : simulation studies
มหาวิทยาลัยเกษตรศาสตร์ Kamolrat Somboon | Prapasiri Pongprayoon Patchreenart Saparpakorn | วิทยานิพนธ์/Thesis |
Prapasiri Pongprayoon
Patchreenart Saparpakorn