Spectroscopic and molecular docking studies on the interaction between spermidine and pancreatic elastase.
Elastase
Kinetics
Protein stability
Quenching
Spermidine
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
15 Jun 2019
15 Jun 2019
Historique:
received:
02
12
2018
revised:
26
02
2019
accepted:
13
03
2019
pubmed:
19
3
2019
medline:
10
9
2019
entrez:
19
3
2019
Statut:
ppublish
Résumé
In this study, the impact of spermidine on the stability, conformation and activity of elastase was investigated at the pH of 8.5 (the optimum pH for elastase) and different temperatures (303, 313, and 323 K) using UV-vis spectrophotometry, Spectrofluorimetry, circular dichroism, and enzyme activity measurements. The empirical results were obtained and compared with those achieved by the molecular docking simulation. Spectrofluorometric results proved that with the addition of spermidine to the protein solution, the emission severity of elastase was extremely reduced. Further, the Stern-Volmer equation demonstrated that quenching was principally of the static type. Moreover, ∆H
Identifiants
pubmed: 30880056
pii: S0141-8130(18)36688-1
doi: 10.1016/j.ijbiomac.2019.03.084
pii:
doi:
Substances chimiques
Pancreatic Elastase
EC 3.4.21.36
Spermidine
U87FK77H25
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
473-483Informations de copyright
Copyright © 2019. Published by Elsevier B.V.