TAILIEUCHUNG - Báo cáo khoa học: The minimal amyloid-forming fragment of the islet amyloid polypeptide is a glycolipid-binding domain

Several proteins that interact with cell surface glycolipids share a common fold with a solvent-exposed aromatic residue that stacks onto a sugar ring of the glycolipid (CH–pstacking interaction). Stacking interactions between aromatic residues (p–pstacking) also play a pivotal role in the assembly pro-cess, including many cases of amyloid fibril formation. | ễFEBS Journal The minimal amyloid-forming fragment of the islet amyloid polypeptide is a glycolipid-binding domain Michal Levy1 Nicolas Garmy2 Ehud Gazit1 and Jacques Fantini2 1 Department of Molecular Microbiology and Biotechnology TelAviv University Israel 2 Universite PaulCezanne Laboratoire de Biochimie et Physicochimie des Membranes Biologiques Faculte des Sciences et Techniques St-Jerome Marseille France Keywords amyloid aromatic stacking CH-p interaction glycolipid suramin Correspondence J. Fantini Universite PaulCezanne Laboratoire de Biochimie et Physicochimie des Membranes Biologiques Faculte des Sciences de St-Jerome 13397 Marseille Cedex 20 France Fax 33 491 288 236 Tel 33 491 28 27 54 E-mail Received 15 September 2006 revised 25 October 2006 accepted 27 October 2006 doi Several proteins that interact with cell surface glycolipids share a common fold with a solvent-exposed aromatic residue that stacks onto a sugar ring of the glycolipid CH p stacking interaction . Stacking interactions between aromatic residues p-p stacking also play a pivotal role in the assembly process including many cases of amyloid fibril formation. We found a structural similarity between a typical glycolipid-binding domain the V3 loop of HIV-1 gp120 and the minimal amyloid-forming fragment of the human islet amyloid polypeptide . the octapeptide core module NFGAILSS. In a monolayer assay at the air-water interface the NFGAILSS peptide specifically interacted with the glycolipid lactosylceramide. The interaction appears to require an aromatic residue as NLGAILSS was poorly recognized by lactosylceramide whereas NYGAILSS behaved like NFGAILSS. In addition we observed that the full-length human islet amyloid polypeptide 1-37 did interact with a monolayer of lactosylceramide and that the glycolipid film significantly affected the aggregation process of the peptide. As glycolipid-V3 interactions are efficiently .

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