PMID- 32432078
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20200928
IS  - 2296-2646 (Print)
IS  - 2296-2646 (Electronic)
IS  - 2296-2646 (Linking)
VI  - 8
DP  - 2020
TI  - Applications of Mass Spectrometry in the Onset of Amyloid Fibril Formation: Focus 
      on the Analysis of Early-Stage Oligomers.
PG  - 324
LID - 10.3389/fchem.2020.00324 [doi]
LID - 324
AB  - Amyloid fibril formation is a hallmark of diverse neurodegenerative and metabolic 
      diseases, such as Alzheimer's disease (AD), Parkinson's disease (PD), and type 2 
      diabetes mellitus (T2DM). Conventional diagnosis is based on the appearance of 
      fibrils or plaques, while neglects the role of early-stage oligomers in the 
      disease progression. Recent studies have uncovered that it is the early-stage 
      oligomer, rather than the mature fibril, that greatly contributes cytotoxicity. 
      The formation of oligomers involves complicate structural conversions and it is 
      essential to investigate their conformational changes for a better understanding 
      of aggregation mechanism. The coexistence of soluble early-stage oligomers, 
      intermediates, and pre-fibril species makes it difficult to be differentiate by 
      morphological methods, and only average structural information is provided as 
      they lack the ability of separation. Therefore, mass spectrometry (MS) becomes an 
      alternative technique that presents new and complementary insights into the onset 
      of amyloid fibrils. This review highlights the hotspots and important 
      achievements by MS in the field of amyloid formation mechanism, including the 
      direct detection and differentiation of soluble oligomers (native MS), 
      unambiguous identification of interacted sites involved in the onset of 
      aggregation [hydrogen/deuterium exchange (HDX) and chemical cross-linking (CX)], 
      and conformational switch that leads to fibrilization [collision cross section 
      (CCS) regularity by ion mobility (IM)].
CI  - Copyright (c) 2020 Hu and Zheng.
FAU - Hu, Jiaojiao
AU  - Hu J
AD  - Key Laboratory of Drug Metabolism and Pharmacokinetics, State Key Laboratory of 
      Natural Medicines, Department of Pharmaceutical Analysis, School of Pharmacy, 
      China Pharmaceutical University, Nanjing, China.
FAU - Zheng, Qiuling
AU  - Zheng Q
AD  - Key Laboratory of Drug Metabolism and Pharmacokinetics, State Key Laboratory of 
      Natural Medicines, Department of Pharmaceutical Analysis, School of Pharmacy, 
      China Pharmaceutical University, Nanjing, China.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20200505
PL  - Switzerland
TA  - Front Chem
JT  - Frontiers in chemistry
JID - 101627988
PMC - PMC7215083
OTO - NOTNLM
OT  - aggregation mechanism
OT  - amyloid fibril
OT  - conformational analysis
OT  - early-stage oligomers
OT  - mass spectrometry
EDAT- 2020/05/21 06:00
MHDA- 2020/05/21 06:01
PMCR- 2020/01/01
CRDT- 2020/05/21 06:00
PHST- 2019/10/22 00:00 [received]
PHST- 2020/03/30 00:00 [accepted]
PHST- 2020/05/21 06:00 [entrez]
PHST- 2020/05/21 06:00 [pubmed]
PHST- 2020/05/21 06:01 [medline]
PHST- 2020/01/01 00:00 [pmc-release]
AID - 10.3389/fchem.2020.00324 [doi]
PST - epublish
SO  - Front Chem. 2020 May 5;8:324. doi: 10.3389/fchem.2020.00324. eCollection 2020.