Super-Temporal-Resolved Microscopy Reveals Multistep Desorption Kinetics of α-Lactalbumin from Nylon

Langmuir : the ACS Journal of Surfaces and Colloids
Wenxiao WangChristy F Landes

Abstract

Insight into the mechanisms driving protein-polymer interactions is constantly improving due to advances in experimental and computational methods. In this study, we used super-temporal-resolved microscopy (STReM) to study the interfacial kinetics of a globular protein, α-lactalbumin (α-LA), adsorbing at the water-nylon 6,6 interface. The improved temporal resolution of STReM revealed that residence time distributions involve an additional step in the desorption process. Increasing the ionic strength in the bulk solution accelerated the desorption rate of α-LA, attributed to adsorption-induced conformational changes. Ensemble circular dichroism measurements were used to support a consecutive reaction mechanism. Without the improved temporal resolution of STReM, the desorption intermediate was not resolvable, highlighting both STReM's potential to uncover new kinetic mechanisms and the continuing need to push for better time and space resolution.

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Citations

Oct 30, 2019·Proceedings of the National Academy of Sciences of the United States of America·Nicholas A MoringoChristy F Landes
Feb 9, 2019·Optics Express·Wenxiao WangChristy F Landes
Aug 23, 2018·Accounts of Chemical Research·Logan D C Bishop, Christy F Landes
Sep 17, 2020·Analytical Chemistry·William CalabraseLydia Kisley
Aug 14, 2020·Analytical Chemistry·Manhua PanTai-Yen Chen
Oct 24, 2018·Analytical Chemistry·Herman CoceancighTakashi Ito
Feb 23, 2020·Langmuir : the ACS Journal of Surfaces and Colloids·Nicholas A MoringoChristy F Landes

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