Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant

GADDI, G. M.; GISONNO, R.; ROSÚ, S A.; CORTEZ, M. F; FINARELLI, G. S.; RAMELLA, N.; TRICERRI, M. A.

Data in Brief

ELSEVIER SCIENCE INC

Lugar: Pensilvania; Año: 2020

2352-3409

The article shows dataset of the proteolysis of a natural variant of apolipoprotein A-I (apoA-I)with a substitution of a leucine by and arginine in position 60 (L60R), in comparison with the proteinwith the native sequence (Wt). This information demonstrates the potential of in vitro partial proteolysisexperiments as it may be applicable to different approaches in the biophysical field. We have analyzedby different electrophoresis techniques apoA-I variants, quantified the degree of proteolysis afterstaining and compared the proteolysis efficiency with the computed cleavage patterns. The data shownhere clearly strengthen the usefulness of this approach to test protein flexibility, as it may be attainedwith enzymes which are not expected to modify in vivo this protein but have a well-known digestionpattern. In addition it is appropriate for evaluating protein catabolism, as it is exemplified here by theevidence with metalloproteinase 12 (MMP-12), which is a physiological protease that may elicit the proinflammatoryprocessing of this variant within the lesions. We support the work ?Structural analysis of anatural apolipoprotein A-I variant (L60R) associated with amyloidosis? (Gaddi, GM et al Arch. Biochem.Biophys. 685 (2020). doi:10.1016/j.abb.2020.108347), gaining insights on protein folding from acharacterization by proteolysis analysis [1].