Aqueous alkaline phosphate facilitates the non-exchangeable deuteration of peptides and proteins.
RSC Adv
; 14(12): 8075-8080, 2024 Mar 06.
Article
in En
| MEDLINE
| ID: mdl-38464689
ABSTRACT
The incorporation of deuterium into peptides and proteins holds broad applications across various fields, such as drug development and structural characterization. Nevertheless, current methods for peptide/protein deuteration often target exchangeable labile sites or require harsh conditions for stable modification. In this study, we present a late-stage approach utilizing an alkaline phosphate solution to achieve deuteration of non-exchangeable backbone sites of peptides and proteins. The specific deuteration regions are identified through ultraviolet photodissociation (UVPD) and mass spectrometry analysis. This deuteration strategy demonstrates site and structure selectivity, with a notable affinity for labeling the α-helix regions of myoglobin. The deuterium method is particularly suitable for peptides and proteins that remain stable under high pH conditions.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
RSC Adv
Year:
2024
Document type:
Article