Multiplatform High-Definition Ion Mobility Separations of the Largest Epimeric Peptides.
Anal Chem
; 96(6): 2318-2326, 2024 02 13.
Article
en En
| MEDLINE
| ID: mdl-38301112
ABSTRACT
Ion mobility spectrometry (IMS) coupled to mass spectrometry (MS) has become a versatile tool to fractionate complex mixtures, distinguish structural isomers, and elucidate molecular geometries. Along with the whole MS field, IMS/MS advances to ever larger species. A topical proteomic problem is the discovery and characterization of d-amino acid-containing peptides (DAACPs) that are critical to neurotransmission and toxicology. Both linear IMS and FAIMS previously disentangled d/l epimers with up to â¼30 residues. In the first study using all three most powerful IMS methodologiesâtrapped IMS, cyclic IMS, and FAIMSâwe demonstrate baseline resolution of the largest known d/l peptides (CHH from Homarus americanus with 72 residues) with a dynamic range up to 100. This expands FAIMS analyses of isomeric modified peptides, especially using hydrogen-rich buffers, to the â¼50-100 residue range of small proteins. The spectra for d and l are unprecedentedly strikingly similar except for a uniform shift of the separation parameter, indicating the conserved epimer-specific structural elements across multiple charge states and conformers. As the interepimer resolution tracks the average for smaller DAACPs, the IMS approaches could help search for yet larger DAACPs. The a priori method to calibrate cyclic (including multipass) IMS developed here may be broadly useful.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Proteómica
Idioma:
En
Revista:
Anal Chem
Año:
2024
Tipo del documento:
Article
País de afiliación:
Estados Unidos