Optical Detection of Interleukin-6 Using Liquid Janus Emulsions Using Hyperthermophilic Affinity Proteins

Thumbnail Image
Download
Name

optical-detection-of-interleukin-6-using-liquid-janus-emulsions-using-hyperthermophilic-affinity-proteins.pdf

Description
Published version
Size

15.25 MB

Format

Adobe PDF

Checksum (MD5)

6c3244bc9ad83cdbd2e1f1c285e00bee

Thumbnail Image
Download
Name

correction-to-optical-detection-of-interleukin-6-using-liquid-janus-emulsions-using-hyperthermophilic-affinity-proteins.pdf

Description
Correction
Size

1.06 MB

Format

Adobe PDF

Checksum (MD5)

187c622e3dc79ddfa84adcd2b9805723

sword-2025-12-12T22:22:11.original.xml (130 B)
Original SWORD entry document
Author(s)
Chen, Michelle
•
Corless, Elliot I
•
Engelward, Bevin P
•
Swager, Timothy M
•
Sikes, Hadley D.
Date Issued
August 22, 2024
Journal
ACS Omega
Publisher
American Chemical Society
Citation
Chen, Michelle, Corless, Elliot I, Engelward, Bevin P, Swager, Timothy M and Sikes, Hadley D. 2024. "Optical Detection of Interleukin-6 Using Liquid Janus Emulsions Using Hyperthermophilic Affinity Proteins." ACS Omega, 9 (35).
Version
Final published version
Abstract
When equal volumes of two immiscible liquids are mixed (e.g., a hydrocarbon and a fluorocarbon), Janus droplets can form in an aqueous solution. In a gravity-aligned Janus droplet, the boundary between the two phases is flat and thus optically transparent when viewed from above. When tipped due to interactions with an analyte (i.e., agglutination), the resulting change in refraction and reflection yields an optical signal that can be detected and quantified. This study reports the detection and quantitation of interleukin-6 (IL-6) using emulsions functionalized at the hydrocarbon:aqueous interface with engineered proteins that bind IL-6 at high affinity and specificity. Hyperthermophilic affinity proteins (rcSso7d) are derived from thermophiles, giving them excellent thermal stability. Two rcSso7d affinity protein variants were synthesized with a noncanonical azide-functionalized amino acid to enable click chemistry to novel polymeric anchors embedded in the hydrocarbon phase. The two binding proteins recognize different epitopes, enabling the detection of both monomeric and dimeric IL-6 via agglutination. It is noteworthy that the rsSso7d protein variants, in addition to having superior thermal stability and facile recombinant synthesis in E. coli, show superior performance when compared to commercial antibodies for IL-6.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivatives
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/acsomega.4c03959
PrivacyPermissionsAccessibilityContact us
Notify us about copyright concerns.