Structural peculiarities of lysozyme - PLURONIC complexes at the aqueous-air and liquid-liquid interfaces and in the bulk of aqueous solution.
Lysozyme
Lysozyme-Pluronic complex
Pluronic copolymers
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:
05 May 2020
05 May 2020
Historique:
received:
25
02
2020
revised:
23
04
2020
accepted:
24
04
2020
pubmed:
11
5
2020
medline:
11
5
2020
entrez:
11
5
2020
Statut:
aheadofprint
Résumé
Interaction between proteins and synthetic polymers that represent a perspective potential in drug delivery or/and already used in medicine plays a key role in biological functioning of both molecules along with a system as a whole. In present study association between hen egg white lysozyme and Pluronic triblock-copolymers (L121, P123 and F127) in the bulk of the solution as well as at the aqueous-air and liquid-liquid interfaces was analyzed by means of spectroscopic and radiochemical assay. In protein-Pluronic complexes lysozyme keeps the secondary structure (CD and SAXS data results), while fluorescence and UV-analysis indicates changes in the local surrounding of fluorophoric amino acid residues. Radiochemical assay in combination with molecular docking reveals the formation of the complexes, in which proline residues turned to the interface between water and hydrophobic medium.
Identifiants
pubmed: 32387357
pii: S0141-8130(20)33088-9
doi: 10.1016/j.ijbiomac.2020.04.221
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
721-731Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.