Your browser does not allow JavaScript!
JavaScript is necessary for the proper functioning of this website. Please enable JavaScript or use a modern browser.
Open Science Slovenia
Open Science
DiKUL
slv
|
eng
Search
Browse
New in RUL
About RUL
In numbers
Help
Sign in
Targeting N-acetylglucosaminidase in Staphylococcus aureus with iminosugar inhibitors
ID
Sluga, Janja
(
Author
),
ID
Tomašič, Tihomir
(
Author
),
ID
Anderluh, Marko
(
Author
),
ID
Hrast, Martina
(
Author
),
ID
Bajc, Gregor
(
Author
),
ID
Sevšek, Alen
(
Author
),
ID
Martin, Nathaniel I.
(
Author
),
ID
Pieters, Roland J.
(
Author
),
ID
Novič, Marjana
(
Author
),
ID
Venko, Katja
(
Author
)
PDF - Presentation file,
Download
(1,88 MB)
MD5: 8D429F08799F0CEBD3DD63A8006B1B24
URL - Source URL, Visit
https://www.mdpi.com/2079-6382/13/8/751
Image galllery
Abstract
Bacteria are capable of remarkable adaptations to their environment, including undesirable bacterial resistance to antibacterial agents. One of the most serious cases is an infection caused by multidrug-resistant Staphylococcus aureus, which has unfortunately also spread outside hospitals. Therefore, the development of new effective antibacterial agents is extremely important to solve the increasing problem of bacterial resistance. The bacteriolytic enzyme autolysin E (AtlE) is a promising new drug target as it plays a key role in the degradation of peptidoglycan in the bacterial cell wall. Consequently, disruption of function can have an immense impact on bacterial growth and survival. An in silico and in vitro evaluation of iminosugar derivatives as potent inhibitors of S. aureus (AtlE) was performed. Three promising hit compounds (1, 3 and 8) were identified as AtlE binders in the micromolar range as measured by surface plasmon resonance. The most potent compound among the SPR response curve hits was 1, with a K$_D$ of 19 μM. The K$_D$ value for compound 8 was 88 μM, while compound 3 had a K$_D$ value of 410 μM.
Language:
English
Keywords:
autolysin E
,
glycoside hydrolase
,
iminosugars
,
surface plasmon resonance
,
enzyme inhibition
Work type:
Article
Typology:
1.01 - Original Scientific Article
Organization:
FFA - Faculty of Pharmacy
BF - Biotechnical Faculty
Publication status:
Published
Publication version:
Version of Record
Year:
2024
Number of pages:
12 str.
Numbering:
Vol. 13, iss. 8, art. 751
PID:
20.500.12556/RUL-160064
UDC:
615.015.8
ISSN on article:
2079-6382
DOI:
10.3390/antibiotics13080751
COBISS.SI-ID:
204113923
Publication date in RUL:
14.08.2024
Views:
133
Downloads:
24
Metadata:
Cite this work
Plain text
BibTeX
EndNote XML
EndNote/Refer
RIS
ABNT
ACM Ref
AMA
APA
Chicago 17th Author-Date
Harvard
IEEE
ISO 690
MLA
Vancouver
:
Copy citation
Share:
Record is a part of a journal
Title:
Antibiotics
Shortened title:
Antibiotics
Publisher:
MDPI AG
ISSN:
2079-6382
COBISS.SI-ID:
522975769
Licences
License:
CC BY 4.0, Creative Commons Attribution 4.0 International
Link:
http://creativecommons.org/licenses/by/4.0/
Description:
This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.
Secondary language
Language:
Slovenian
Keywords:
avtolizin E
,
glikozid hidrolaza
,
iminosladkorji
,
površinska plazmonska resonanca
,
zaviranje encimov
,
bakterijska rezistenca
Projects
Funder:
ARIS - Slovenian Research and Innovation Agency
Project number:
P1-0017
Name:
Modeliranje kemijskih procesov in lastnosti spojin
Funder:
Other - Other funder or multiple funders
Project number:
39008
Name:
Young researchers fund
Similar documents
Similar works from RUL:
Similar works from other Slovenian collections:
Back