Human-derived voltage-gated potassium channel 1.3 immunogenic peptide fragment and application thereof

Abstract

The invention provides a human-derived voltage-gated potassium channel 1.3 immunogenic peptide fragment and applications thereof. The peptide is composed of 13 continuous amino acids on an extracellular loop between an alpha subunit transmembrane fragment S5 and S6 of human-derived voltage-gated potassium channel 1.3. The amino acid sequence of the peptide fragment is Glu-Ala-Asp-Asp-Pro-Thr-Ser-Gly-Phe-Ser-Ser-Ile-Pro-Asp. An antibody against the peptide fragment prepared by an immunological method can be used as a new, specific inhibitor of human-derived voltage-gated potassium channel 1.3,and the antibody can be used in a study for regulating functions of human-derived voltage-gated potassium channel 1.3. Monoclonal antibodies and vaccines prepared based on the above peptide fragment facilitate the treatment of autoimmune diseases or autoimmune related diseases.

Description

technical field [0001] The invention belongs to the field of biotechnology, and relates to a human-derived voltage-gated potassium channel 1.3 immunogenic peptide and its application. The English full name of this channel is human voltage-gated potassium channel 1.3, hereinafter referred to as hKv1.3. The antibody prepared by using hKv1.3 channel extracellular loop peptide E314, hereinafter referred to as anti-hKv1.3 extracellular loop peptide E314 antibody, can be used as a new and specific inhibitor of hKv1.3 channel. Background technique [0002] Voltage-gated potassium channels are a class of transmembrane proteins that allow potassium ions to pass through cell membranes. They play a role in bioelectric signal transduction of excitable and non-excitable cells such as neurons, muscle cells and lymphocytes. The Kv1.3 channel, one of the members of the voltage-gated potassium channel family, has been confirmed to be abundantly distributed in some specific regions of immun...

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Problems solved by technology

Studies have found that the binding sites of Kv1.3 channels and cardiac repolarization HERG and KCNQ1 / KCNE1 potassium channel blockers are highly conserved, which makes some existing Kv1.3 channel blockers block Kv1.3 channels at the same time , and also block HERG and KCNQ1 / KCNE1 channels, often leading to the occurrence of drug-induced arrhythmias, which hinders the further development of some Kv1.3 channel blockers into clinical drugs

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