6-mer Peptide Selectively Anneals to a Pathogenic Serpin Conformation and Blocks Polymerization
نویسندگان
چکیده
منابع مشابه
Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells.
Blockade of Kv1.3 K(+) channels in T cells is a promising therapeutic approach for the treatment of autoimmune diseases such as multiple sclerosis and type 1 diabetes mellitus. Vm24 (α-KTx 23.1) is a novel 36-residue Kv1.3-specific peptide isolated from the venom of the scorpion Vaejovis mexicanus smithi. Vm24 inhibits Kv1.3 channels of human lymphocytes with high affinity (K(d) = 2.9 pM) and e...
متن کاملVm24, a natural immunosuppressant peptide potently and selectively blocks Kv1.3 potassium channels of human T cells
Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, Debrecen, Hungary, 4032: Z.V., F.P, R.G., G.P Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnologia, Universidad Nacional Autónoma de México, Cuernavaca, Mexico 62210: G.G-B, G.P-A, Y.R., L.D.P. Ecologie, Systématique et Evolution, Université Paris-Sud, F-91405, Orsa...
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15 صفحه اولSerpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization
The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Serpins play absolutely critical role in the control of proteases involved in the inflammatory, complement, coagulation and fibrinolytic pathways and are associated with many conformational dis...
متن کاملPolymerization of a peptide-based enzyme substrate.
Polymers of norbornenyl-modified peptide-based enzyme substrates have been prepared via ring-opening metathesis polymerization (ROMP). Peptides displayed on water-soluble homopolymers retain the ability to be enzymatically processed by a disease-associated enzyme. In contrast, when the peptides are densely arrayed on a nanoparticle derived from a self-assembled amphiphilic block-copolymer, they...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.c100722200