HA2 peptide

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HA2 peptide is a potent pH-responsive fusion peptide derived from hemagglutinin (HA), corresponding to the N-terminal fusion peptide domain consisting of 23 amino acid residues of HIV-1 gp41 envelope glycoprotein. HA2 peptide adopts a random coil structure under physiological pH conditions; in acidic endosomes, protonation of carboxyl groups reduces negative charge, inducing a transition to an α-helical conformation that can fuse with and destabilize the endosomal membrane. After binding to membranes, the N-terminal and middle regions of HA2 peptide mainly adopt a β-strand conformation, while the C-terminal region remains unstructured. HA2 peptide induces lipid mixing and promotes aqueous content leakage from large unilamellar vesicles whose lipid composition matches that of HIV-1 viruses and target T cells. HA2 peptide is anionic and can bind to cationic peptides to achieve siRNA condensation. HA2 peptide can be used in studies related to cancer and human immunodeficiency virus (HIV) infection.

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