Core–Shell Gold Nanoparticles as Non-Conventional Matrix for the MALDI-ToF-MS Detection of Amino Acids: A Preliminary Study

2008 ◽  
Vol 6 (4) ◽  
pp. 654-661 ◽  
Author(s):  
N. Cioffi ◽  
F. De Palo ◽  
C. D. Calvano ◽  
I. D. van der Werf ◽  
F. Palmisano ◽  
...  
2015 ◽  
Vol 3 (48) ◽  
pp. 9330-9339 ◽  
Author(s):  
Xing-yu Long ◽  
Qun Song ◽  
Hong-zhen Lian

Lichee-like core–shell structured magnetic lutetium phosphate (Fe3O4@LuPO4) affinity microspheres were synthesized, characterized and successfully applied to enrich phosphopeptides.


2021 ◽  
Author(s):  
Ahmad Shahir Sadr ◽  
zahra abdollahpour ◽  
Atousa Aliahmadi ◽  
Changiz Eslahchi ◽  
Mina Nekouei ◽  
...  

Abstract The hydrogen/deuterium exchange (HDX) is a reliable method to survey the dynamic behavior of proteins and epitope mapping. Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS) is a quantifying tool to assay for HDX in the protein of interest. We combined HDX-MALDI-TOF MS and molecular docking/MD simulation to identify accessible amino acids and analyze their contribution in the structural changes of profilin1 (PFN1). The molecular docking/MD simulations are computational tools for enabling the analysis of the type of amino acids that may be involved via HDX identified under the lowest binding energy condition. Glycine to Valine amino acid (G117V) substitution mutation is linked to amyotrophic lateral sclerosis (ALS). This mutation is found to be in the actin-binding site of PFN1 and prevents the dimerization/polymerization of actin and invokes a pathologic toxicity that leads to ALS. In this study, we sought to understand the PFN1 protein dynamic behavior using purified wild type and mutant PFN1 proteins. The data obtained from HDX-MALDI-TOF MS for PFN1WT and PFN1G117V at various time intervals, from seconds to hours, revealed multiple peaks corresponding to molecular weights from monomers to multimers. PFN1/Benzaldehyde complexes identified 20 accessible amino acids to HDX that participate in the docking simulation in the surface of WT and mutant PFN1. Consistent results from HDX-MALDI-TOF MS and docking simulation predict candidate amino acid(s) involved in the dimerization/polymerization of PFNG117V. This information may shed critical light on the structural and conformational changes with details of amino acid epitopes for mutant PFN1s’ dimerization, oligomerization, and aggregation.


Talanta ◽  
2019 ◽  
Vol 200 ◽  
pp. 288-292 ◽  
Author(s):  
Shuping Long ◽  
Qin Qin ◽  
Yuning Wang ◽  
Yi Yang ◽  
Yan Wang ◽  
...  

2005 ◽  
Vol 4 (5) ◽  
pp. 1863-1866 ◽  
Author(s):  
Laurie L. Parker ◽  
Alexander B. Schilling ◽  
Stephen J. Kron ◽  
Stephen B. H. Kent
Keyword(s):  

2017 ◽  
Vol 137 ◽  
pp. 30-33 ◽  
Author(s):  
Veronika Rotova ◽  
Costas C. Papagiannitsis ◽  
Anna Skalova ◽  
Katerina Chudejova ◽  
Jaroslav Hrabak
Keyword(s):  

The Analyst ◽  
2004 ◽  
Vol 129 (9) ◽  
pp. 817 ◽  
Author(s):  
Xiaoyan Zhao ◽  
Jennifer Barber-Singh ◽  
Scott A. Shippy
Keyword(s):  

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