Surface simulation synthesis: a new strategy to spy alpha-helix structure.
In key proteins, there are always some alpha-helix structures, which play important role in the structure and functions. Many epitopes lie on the surface of alpha-helix. These epitopes are not easy to be recruited into the vaccine development, because they are conformation dependent epitopes. Can such epitopes on alpha-helix be mimicked synthetically? Our findings undoubtedly validate the feasibility of surface simulation synthesis with short linear peptide to mimic the antigenic side of alpha-helix structure.
Dong
Xiao-Nan
XN
Chen
Yu
Y
Chen
Ying-Hua
YH
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000737:chemistry* / Q000276:immunology; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000276:immunology; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000276:immunology; D017433:Protein Structure, Secondary
D000911:Antibodies, Monoclonal; D000939:Epitopes; D015700:HIV Envelope Protein gp41; D010455:Peptides