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Kannika Thongkhao. Structural characterization and mode of action studies of salvicin K and antimicrobial peptide-like bacteriocin B peptides from Lactobacillus salivarius K4. Doctoral Degree(Genetic Engineering). Kasetsart University. Office of the University Library. : Kasetsart University, 2016.
Structural characterization and mode of action studies of salvicin K and antimicrobial peptide-like bacteriocin B peptides from Lactobacillus salivarius K4
Name: Kannika Thongkhao
Classification :.LCCS: QR82.L3
LCSH:
Lactobacillus
LCSH:
Peptide antibiotics
LCSH:
Bacteriocins
LCSH:
Lactic acid bacteria
Abstract:
Salvicin K (Sal K) and antimicrobial peptide-like bacteriocin β (Alb β) are cationic antimicrobial peptides (AMPs) from Lactobacillus salivarius K4. They have been reported as novel bacteriocins from lactic acid bacteria. However, their structures and mode of action are unclear. Hence, in this study we aimed to characterize the structures and mode of action of the Sal K and Alb β peptides. The individual Sal K peptide showed no antimicrobial activity against S. aureus and Streptococcus sp. TISTR1030, while Alb β peptide showed low potent activity against the Gram-positive bacteria with an MIC of 125 µg/mL. Interestingly, the mixture of Sal K and Alb β peptides exhibited 8 times higher antimicrobial activity than that in the individual peptides indicating the synergy between the Sal K and Alb β peptides. Peptide-induced membrane disruption assays showed that the peptide mixture caused cell cytotoxicity and intracellular components leakage. Scanning electron microscope revealed morphological alterations of bacterial cell surface. Moreover, the inner membrane disruptions were observed by transmission electron microscope. Although the structure determination by NMR and CD spectroscopy techniques showed that the individual Sal K and Alb β peptides exhibited random coil conformation in water solution, the 1D-1 H NMR spectra of the peptide mixture showed interaction between Sal K and Alb β peptides. Partitioning coefficients of the peptide-micelles complexes revealed strong binding between peptides with the SDS and DPC micelles systems. Nevertheless, in CD experiment the peptides adopted α-helix structure in SDS micelles, while random coil structures were observed in DPC micelles.
Kasetsart University. Office of the University Library
Address:
Bangkok
Email:
tdckulib@ku.ac.th
Name: Kiattawee Choowongkomon
Role:
Thesis Advisor
Name: Nonlawat Boonyalai
Role:
Thesis Co-Advisor
Created:
2016
Modified:
2023-06-09
Issued:
2023-06-09
วิทยานิพนธ์/Thesis
application/pdf
URL: https://kasetsart.idm.oclc.org/login?url=https://www.lib.ku.ac.th/KUthesis/2559/kannika-tho-all.pdf
CallNumber:
QR82.L3.K36
eng
DegreeName: Doctor of Philosophy
Level: Doctoral Degree
Descipline: Genetic Engineering
Grantor: Kasetsart University
©copyrights Kasetsart University
RightsAccess:
ใช้เวลา
0.027847 วินาที
Kannika Thongkhao
| Title | Contributor | Type |
|---|---|---|
| Structural characterization and mode of action studies of salvicin K and antimicrobial peptide-like bacteriocin B peptides from Lactobacillus salivarius K4
มหาวิทยาลัยเกษตรศาสตร์ Kannika Thongkhao | Kiattawee Choowongkomon Nonlawat Boonyalai | วิทยานิพนธ์/Thesis |
Kiattawee Choowongkomon
Nonlawat Boonyalai