Scaling Proteome-Wide Reactions of Activity-Based Probes.
Anal Chem
; 89(12): 6295-6299, 2017 06 20.
Article
en En
| MEDLINE
| ID: mdl-28570047
ABSTRACT
Unified analysis of complex reactions of an activity-based probe with proteins in a proteome remains an unsolved challenge. We propose a power expression, rate = kobs[Probe]α, for scaling the progress of proteome-wide reactions and use the scaling factor (0 ≤ α ≤ 1) as an apparent, partial order with respect to the probe to measure the "enzyme-likeness" for a protein in reaction acceleration. Thus, α reports the intrinsic reactivity of the protein with the probe. When α = 0, the involved protein expedites the reaction to the maximal degree; when α = 1, the protein reacts with the probe via an unaccelerated, bimolecular reaction. The selectivity (ß) of the probe reacting with two proteins is calculated as a ratio of conversion factors (kobs values) for corresponding power equations. A combination of α and ß provides a tiered system for quantitatively assessing the probe efficacy; an ideal probe exhibits high reactivity with its protein targets (low in α) and is highly selective (high in ß) in forming the probe-protein adducts. The scaling analysis was demonstrated using proteome-wide reactions of HT-29 cell lysates with a model probe of threonine ß-lactone.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Treonina
/
Sondas Moleculares
/
Proteoma
/
Lactonas
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Anal Chem
Año:
2017
Tipo del documento:
Article
País de afiliación:
Estados Unidos