Journal Article FZJ-2026-03563

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png
Surfactant-driven modifications in protein structure

 ;  ;  ;

2025
Royal Soc. of Chemistry London

Soft matter 21(25), 4979 - 4998 () [10.1039/D5SM00207A]

This record in other databases:  

Please use a persistent id in citations: doi:

Abstract: MLZ Grand Challenges: In this review article, we summarize the fundamentals and recent updates on (i) protein interaction with surfactants; (ii) the phenomenon of protein unfolding and refolding, and (iii) the utilization of protein-surfactant interactions to direct heat-induced protein gelation. The protein-surfactant interaction and their resultant complexes have gained significant interest due to its extensive applications across various fields, including the food industry, cosmetics, and medicine. Surfactants are known to unfold the protein, where there are extensive models describing the basic mechanism of such unfolding and the resultant structure formed across micro-to-macro length scales. These models grounded in extensive experimental and simulation studies aim to predict the interaction dynamics based on several physicochemical parameters, such as surfactant properties (e.g., ionic character, tail length), protein characteristics (e.g., charge, isoelectric point), and solution conditions (e.g., pH, ionic strength, temperature). Recently, there has been a growing interest in the refolding of surfactant-induced unfolded proteins using combinations of ionic and nonionic surfactants and some mechanical procedures such as dilution, dialysis, etc. While the mechanisms of such refolding are still being explored, a general consensus suggests preferential binding of ionic surfactants with nonionic surfactants to form mixed micelles, rather than protein-surfactant complexes. It has also been demonstrated that the interaction of protein with surfactants can be effectively utilized to guide the heat-induced gelation of protein.

Keyword(s): Others (1st) ; Soft Condensed Matter (2nd)

Classification:

Contributing Institute(s):
  1. JCNS-4 (JCNS-4)
  2. JCNS-FRM-II (JCNS-FRM-II)
  3. Heinz Maier-Leibnitz Zentrum (MLZ)
  4. Biomakromolekulare Systeme und Prozesse (IBI-4)
Research Program(s):
  1. 6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ) (POF4-6G4) (POF4-6G4)
  2. 632 - Materials – Quantum, Complex and Functional Materials (POF4-632) (POF4-632)
Experiment(s):
  1. No specific instrument

Database coverage:
Medline ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; Essential Science Indicators ; IF < 5 ; JCR ; National-Konsortium ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
Click to display QR Code for this record

The record appears in these collections:
Dokumenttypen > Aufsätze > Zeitschriftenaufsätze
Workflow collections > Öffentliche Einträge
Workflow collections > Publikationsdatenbank
Publications database

 Datensatz erzeugt am 2026-08-30, letzte Änderung am 2026-09-11


Externer link:
Volltext herunterladen
Restricted
Dieses Dokument bewerten:

Rate this document:
1
2
3
 
(Bisher nicht rezensiert)