Sensitive and colorimetric detection of the structural evolution of superoxide dismutase with gold nanoparticles.
The detection and characterization of protein aggregates are critical in terms of advanced diagnostic applications and investigations of protein stability. A variety of analytical methods (e.g., circular dichroism, size exclusion chromatography, and fluorescence microscopy) have been used in this regard, but they are limited in the trace detection of the structural evolution of protein aggregation. Here we report the gold nanoparticle (AuNP)-based highly sensitive and colorimetric detection of the temporal evolution of superoxide dismutase (SOD1) aggregates implicated in the pathology of amyotrophic lateral sclerosis (ALS). For the temporal discrimination of SOD1 aggregation, AuNPs were conjugated with SOD1 monomers (SOD1-AuNPs). Upon exposure of the probes (SOD1-AuNPs) with SOD1 aggregates, significant changes in both surface plasmon resonance spectra and concomitant colors were observed which are attributed to the formation of probe aggregates of variable sizes onto the SOD1 aggregates.
Hong
Surin
S
School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University, Seoul 151-744, Korea.
Choi
Inhee
I
Lee
Suseung
S
Yang
Young In
YI
Kang
Taewook
T
Yi
Jongheop
J
D000042:Absorption; D003124:Colorimetry; D006046:Gold / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D053768:Metal Nanoparticles / Q000737:chemistry*; D011485:Protein Binding; D012680:Sensitivity and Specificity; D013056:Spectrophotometry, Ultraviolet; D013482:Superoxide Dismutase / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D020349:Surface Plasmon Resonance; D013997:Time Factors
D006046:Gold; D013482:Superoxide Dismutase