Protein assembly at the air-water interface studied by fluorescence microscopy
Protein assembly at the air-water interface (AWI) occurs naturally in many biological processes and provides a method for creating biomaterials. However, the factors that control protein self-assembly at the AWI and the dynamic processes that occur during adsorption are still underexplored. Using fl...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1999. - 27(2011), 21 vom: 01. Nov., Seite 12775-81 |
|---|---|
| 1. Verfasser: | |
| Weitere Verfasser: | , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2011
|
| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Proteins Serum Albumin Xanthenes Water 059QF0KO0R Texas red |
| Zusammenfassung: | Protein assembly at the air-water interface (AWI) occurs naturally in many biological processes and provides a method for creating biomaterials. However, the factors that control protein self-assembly at the AWI and the dynamic processes that occur during adsorption are still underexplored. Using fluorescence microscopy, we investigated assembly at the AWI of a model protein, human serum albumin minimally labeled with Texas Red fluorophore. Static and dynamic information was obtained under low subphase concentrations. By varying the solution protein concentration, ionic strength, and redox state, we changed the microstructure of protein assembly at the AWI accordingly. The addition of pluronic surfactant caused phase segregation to occur at the AWI, with fluid surfactant domains and more rigid protein domains revealed by fluorescence recovery after photobleaching experiments. Protein domains were observed to coalesce during this competitive adsorption process |
|---|---|
| Beschreibung: | Date Completed 16.02.2012 Date Revised 02.12.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la203053g |