TY - JOUR
T1 - Super-Temporal-Resolved Microscopy Reveals Multistep Desorption Kinetics of α-Lactalbumin from Nylon
AU - Wang, Wenxiao
AU - Shen, Hao
AU - Moringo, Nicholas A.
AU - Carrejo, Nicole C.
AU - Ye, Fan
AU - Robinson, Jacob T.
AU - Landes, Christy F.
N1 - Funding Information:
C.F.L. thanks the Welch Foundation (C-1787). N.A.M. and N.C.C. acknowledge that this material is based upon the work supported by the National Science Foundation Graduate Research Fellowship Program under Grant no. 1450681. Additionally, we thank Dr. Richard Willson for providing the labeled α-lactalbumin protein. Special thanks also go to L.J. Tauzin and L.D.C. Bishop for their thoughts and discussions.
Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/6/12
Y1 - 2018/6/12
N2 - 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.
AB - 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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U2 - 10.1021/acs.langmuir.8b00686
DO - 10.1021/acs.langmuir.8b00686
M3 - Article
C2 - 29763567
AN - SCOPUS:85047399715
SN - 0743-7463
VL - 34
SP - 6697
EP - 6702
JO - Langmuir
JF - Langmuir
IS - 23
ER -