TY - JOUR
T1 - Rapid and high-throughput colorimetric screening for anti-aggregation reagents of protein conformational diseases by using gold nanoplasmonic particles
AU - Kim, Hye Young
AU - Kwon, Jung A.
AU - Kang, Taewook
AU - Choi, Inhee
N1 - Publisher Copyright:
© 2017 Elsevier Inc.
PY - 2017/5/1
Y1 - 2017/5/1
N2 - Cellular deposition of destabilized proteins and their aggregates is considered one of the most indisputable factors implicated in protein conformational diseases. Here, we report an innovative high-throughput screening method for discovering anti-aggregation reagents out of numerous potential candidates by using gold nanoplasmonic particles. In our method, nanoparticles act as catalytic activators to accelerate protein aggregation and simultaneously exhibit a colorimetric response according to their embedded shape on the protein aggregates. Using this principle, we observed the colorimetric response to the anti-aggregation effect of amyloid β (Aβ) with the naked eye within a few minutes. Investigation of the anti-aggregation effects of select candidates under three different protein aggregation stages showed that the anti-aggregation efficiency could relate to disease progression. Finally, results obtained with spiked samples in cerebrospinal fluid as well as under various denaturation conditions and different Aβ compositions show the feasibility of future personalized medicine considering individual patient's disease progression.
AB - Cellular deposition of destabilized proteins and their aggregates is considered one of the most indisputable factors implicated in protein conformational diseases. Here, we report an innovative high-throughput screening method for discovering anti-aggregation reagents out of numerous potential candidates by using gold nanoplasmonic particles. In our method, nanoparticles act as catalytic activators to accelerate protein aggregation and simultaneously exhibit a colorimetric response according to their embedded shape on the protein aggregates. Using this principle, we observed the colorimetric response to the anti-aggregation effect of amyloid β (Aβ) with the naked eye within a few minutes. Investigation of the anti-aggregation effects of select candidates under three different protein aggregation stages showed that the anti-aggregation efficiency could relate to disease progression. Finally, results obtained with spiked samples in cerebrospinal fluid as well as under various denaturation conditions and different Aβ compositions show the feasibility of future personalized medicine considering individual patient's disease progression.
KW - Anti-aggregation reagent
KW - Colorimetric sensor
KW - Gold nanoplasmonic particle
KW - High-throughput screening
KW - Protein conformational disease
UR - http://www.scopus.com/inward/record.url?scp=85018506882&partnerID=8YFLogxK
U2 - 10.1016/j.nano.2017.01.004
DO - 10.1016/j.nano.2017.01.004
M3 - Article
C2 - 28115249
AN - SCOPUS:85018506882
SN - 1549-9634
VL - 13
SP - 1575
EP - 1585
JO - Nanomedicine: Nanotechnology, Biology, and Medicine
JF - Nanomedicine: Nanotechnology, Biology, and Medicine
IS - 4
ER -