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

Autor(es)

Micheletto, Mariana C. ; Mendes, Luis F. S. ; Basso, Luis G. M. ; Fonseca-Maldonado, Raquel G. ; Costa-Filho, Antonio J.

• Tipo de documento: Artigo Científico
• Fonte: International Journal of Biological Macromolecules; v. 102, p. 284-293, SEP 2017.
• Citações Web of Science: 2

Resumo

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)

• Processo FAPESP: 12/13309-7 - Estudos estruturais e funcionais da Proteína de Organização e Compactação do Golgi (GRASP) de Cryptococcus neoformans
• Beneficiário: Luis Felipe Santos Mendes
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 15/50366-7 - Resolving mechanistic details of peptide transport across membranes using crystallographic and non-crystallographic structural biology approaches
• Beneficiário: Antonio José da Costa Filho
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 14/00206-0 - Estrutura e função dos peptídeos de fusão da glicoproteína spike do SARS-CoV
• Beneficiário: Luís Guilherme Mansor Basso
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 15/18390-5 - Ressonância magnética eletrônica em biofísica molecular: novos e velhos olhares para novos e velhos problemas
• Beneficiário: Antonio José da Costa Filho
• Modalidade de apoio: Auxílio à Pesquisa - Regular