117138-19-9

HA2 peptide Chemical Structure
117138-19-9

Chemical Structure

HA2 peptide

  • CAS No.: 117138-19-9
  • Formula:C116H158N26O32S
  • Molecular Weight:2460.72

SMILES: O=C(N[C@@H](CC(C)C)C(N[C@@H](CC1=CC=CC=C1)C(NCC(N[C@@H](C)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](C)C(NCC(N[C@@H](CC2=CC=CC=C2)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CCC(O)=O)C(N[C@@H](CC(N)=O)C(NCC(N[C@@H](CC3=CNC4=CC=CC=C34)C(N[C@@H](CCC(O)=O)C(NCC(N[C@@H](CCSC)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CC(O)=O)C(NCC(N[C@@H](CC5=CNC6=CC=CC=C56)C(N[C@@H](CC7=CC=C(C=C7)O)C(NCC(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)CN

Biological Activity: 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[1][2].

Cat. No. Product Name Purity Description Pricing
HY-P11353
HA2 peptide 98.37% 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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