Proteomics

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Comparison of efficacy in immunfopeptide identification from HCT116 by "with" FAIMS

ABSTRACT: HLA class I immunopeptides were affinity purified by W6/32 antibody and analyzed by Orbitrap Fusion Lumos with FAIMS. Customized database which includes somatic mutations of HCT116 obtained from COSMIC database was used for database search. Identification results were filtered at 1% FDR threshold by searching against a randomized decoy database using Proteome Discoverer 2.4 (Sequest HT).

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Koji UEDA 

PROVIDER: PXD023771 | JPOST Repository | Sat Aug 20 00:00:00 BST 2022

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
191216_HCT116_HLAp_1ul(5e6)_CVSet1_PepGr.xlsx Xlsx
191216_HCT116_HLAp_1ul(5e6)_CVSet2_PepGr.xlsx Xlsx
191216_HCT116_HLAp_1ul(5e6)_CVSet3_PepGr.xlsx Xlsx
191216_HCT116_HLAp_1ul_CVSet1.raw Raw
191216_HCT116_HLAp_1ul_CVSet2.raw Raw
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Publications

Differential ion mobility mass spectrometry in immunopeptidomics identifies neoantigens carrying colorectal cancer driver mutations.

Minegishi Yuriko Y   Kiyotani Kazuma K   Nemoto Kensaku K   Inoue Yoshikage Y   Haga Yoshimi Y   Fujii Risa R   Saichi Naomi N   Nagayama Satoshi S   Ueda Koji K  

Communications biology 20220818 1

Understanding the properties of human leukocyte antigen (HLA) peptides (immunopeptides) is essential for precision cancer medicine, while the direct identification of immunopeptides from small biopsies of clinical tissues by mass spectrometry (MS) is still confronted with technical challenges. Here, to overcome these hindrances, high-field asymmetric waveform ion mobility spectrometry (FAIMS) is introduced to conduct differential ion mobility (DIM)-MS by seamless gas-phase fractionation optimal  ...[more]

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