RNase A Domain-Swapped Dimers Produced Through Different Methods: Structure–Catalytic Properties and Antitumor Activity

RNase A Domain-Swapped Dimers Produced Through Different Methods: Structure–Catalytic Properties and Antitumor Activity

Upon oligomerization, RNase A can acquire important properties, such as cytotoxicity against leukemic cells. When lyophilized from 40% acetic acid solutions, the enzyme self-associates through the so-called three-dimensional domain swapping (3D-DS) mechanism involving both N- and/or C-terminals. The...

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Bibliographic Details
Main Authors: Riccardo Montioli, Rachele Campagnari, Sabrina Fasoli, Andrea Fagagnini, Andra Caloiu, Marcello Smania, Marta Menegazzi, Giovanni Gotte
Format: Article
Language:English
Published: MDPI AG 2021-02-01
Series:Life
Subjects:
RNase A
RNase A dimers
3D domain swapping
enzymatic activity
cytotoxic activity
melanoma cells
Online Access:https://www.mdpi.com/2075-1729/11/2/168

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