The 11-mer repeats of human alpha-synuclein in vesicle interactions and lipid composition discrimination: a cooperative role.
alpha-Synuclein is a protein abundant in presynaptic terminals in the brain. The N-terminal region of the sequence contains an imperfect 11-residue periodicity also found in A-class apolipoproteins and able to fold into an amphipathic helix. Here, the ability of three fragments of the protein, which include one, two, and all repeats, respectively, to bind to vesicles of different phospholipid composition is described. The results suggest a cooperative action of the repeats in selecting target membranes for interaction based on their lipid composition. This deduction is possibly related to the physiological role of the protein, which is still poorly understood.
Bisaglia
Marco
M
Institute for Biomolecular Chemistry, CNR, Department of Chemical Sciences, University of Padova, Italy.
Schievano
Elisabetta
E
Caporale
Andrea
A
Peggion
Evaristo
E
Mammi
Stefano
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D002942:Circular Dichroism; D006801:Humans; D050356:Lipid Metabolism; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010743:Phospholipids / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet; D051844:alpha-Synuclein / Q000737:chemistry* / Q000378:metabolism*
D000596:Amino Acids; D008081:Liposomes; D010743:Phospholipids; D051844:alpha-Synuclein