In silico design of mimosine containing peptides as new efficient chelators of aluminum.

ABSTRACT: The design of new and efficient chelators that can remove aluminium(iii), a metal with increasing recognition as a potential toxic agent, from biological systems is an area of high therapeutic relevance. In the present paper, we present an extensive computational study of a new promising type of these chelators based on mimosine containing peptides. The reason to choose mimosine is that the sidechain of this residue is similar to deferiprone, a ligand known to tightly interact with highly-valent metals, and in particular with Al(iii). In this article we analyze systematically, using a combination of methods that include QM/MM MD simulations, how the size and sequence of the polypeptides can alter the fundamental binding patterns to aluminum, in comparison with the binding to deferiprone. P

SUBMITTER: Mujika JI 

PROVIDER: S-EPMC9061177 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature