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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability

Full text
Author(s):
Micheletto, Mariana C. ; Mendes, Luis F. S. ; Basso, Luis G. M. ; Fonseca-Maldonado, Raquel G. ; Costa-Filho, Antonio J.
Total Authors: 5
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 102, p. 284-293, SEP 2017.
Web of Science Citations: 2
Abstract

Acyl-CoA Binding Proteins (ACBP) form a housekeeping family of proteins that is responsible for the buffering of long chain acyl-coenzyme A esters (LCFA-CoA) inside the cell. Even though numerous studies have focused on the characterization of different members of the ACBP family, the knowledge about the impact of both LCFA-CoA and phospholipids on ACBP structure and stability remains scarce. Besides, there are still controversies regarding the possible interaction of ACBP with biological membranes, even though this might be essential for the cargo capture and delivery. In this study, we observed that LCFA-CoA and phospholipids play opposite roles on protein stability and that the interaction with the membrane is dictated by electrostatic interaction. Furthermore, the results support the hypothesis that the LCFA-CoA delivery is driven by the increase of the negative charge on the membrane surface. The combined influence played by the different molecules on ACBP structure is discussed on the light of cargo capture/delivery giving new insights about this important process. (C) 2017 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 12/13309-7 - Structural and functional studies of the Golgi Re-Assembly and Stacking Protein (GRASP) from Cryptococcus neoformans
Grantee:Luis Felipe Santos Mendes
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 14/00206-0 - Structure and function of SARS-CoV spike glycoprotein fusion peptides
Grantee:Luís Guilherme Mansor Basso
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 15/18390-5 - Electron magnetic resonance in molecular biophysics: new and old looks to new and old problems
Grantee:Antonio José da Costa Filho
Support type: Regular Research Grants
FAPESP's process: 15/50366-7 - Resolving mechanistic details of peptide transport across membranes using crystallographic and non-crystallographic structural biology approaches
Grantee:Antonio José da Costa Filho
Support type: Regular Research Grants