title: Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability.
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.
authors.affiliation: Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Mariana C
authors.initials: MC
authors.lastname: Micheletto
authors.affiliation: Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Luís F S
authors.initials: LFS
authors.lastname: Mendes
authors.affiliation: Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
authors.forename: Luis G M
authors.initials: LGM
authors.lastname: Basso
authors.affiliation: Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil; Instituto Federal de Educação, Ciência e Tecnologia de São Paulo/IFSP Campus Jacareí-Dept Gestão, Brazil.
authors.forename: Raquel G
authors.initials: RG
authors.lastname: Fonseca-Maldonado
authors.affiliation: Laboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil. Electronic address: ajcosta@ffclrp.usp.br.
authors.forename: Antonio J
authors.initials: AJ
authors.lastname: Costa-Filho
mesh_terms: D000214:Acyl Coenzyme A / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D000595:Amino Acid Sequence; D026261:Diazepam Binding Inhibitor / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004952:Esters / Q000737:chemistry*; D009154:Mutation; D044367:Phase Transition; D010743:Phospholipids / Q000737:chemistry*; D055550:Protein Stability / Q000187:drug effects; D017433:Protein Structure, Secondary / Q000187:drug effects
chemical_list: D000214:Acyl Coenzyme A; D026261:Diazepam Binding Inhibitor; D004952:Esters; D010743:Phospholipids
keywords: Acyl-CoA binding protein; Protein-ligand interaction; Spectroscopy