Journal Article PUBDB-2020-03356

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Structural peculiarities of lysozyme – PLURONIC complexes at the aqueous-air and liquid-liquid interfaces and in the bulk of aqueous solution

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2020
Elsevier New York, NY [u.a.]

International journal of biological macromolecules 158, 721 - 731 () [10.1016/j.ijbiomac.2020.04.221]
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Abstract: 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.

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Contributing Institute(s):
  1. EMBL-User (EMBL-User)
Research Program(s):
  1. 6G3 - PETRA III (POF3-622) (POF3-622)
Experiment(s):
  1. PETRA Beamline P12 (PETRA III)

Appears in the scientific report 2020
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Medline ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2020-09-11, last modified 2025-07-29


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