Document 0636
 DOCN  M9460636
 TI    NMR-derived solution conformations of a hybrid synthetic peptide
       containing multiple epitopes of envelope protein gp120 from the RF
       strain of human immunodeficiency virus.
 DT    9404
 AU    de Lorimier R; Moody MA; Haynes BF; Spicer LD; Department of
       Biochemistry, Duke University Medical Center,; Durham, North Carolina
       27710.
 SO    Biochemistry. 1994 Mar 1;33(8):2055-62. Unique Identifier : AIDSLINE
       MED/94162209
 AB    Solution conformations of a 40-residue hybrid peptide containing
       T-helper epitopes and B-cell determinants from envelope glycoprotein
       gp120 of human immunodeficiency virus (HIV) have been investigated with
       NMR. Peptides of this general design are highly immunogenic and induce
       HIV-neutralizing antibodies and T-lymphocyte responses. The 16-residue
       N-terminal segment of the peptide contains a T-helper epitope, while the
       24-residue C-terminal segment is derived from the V3 loop of HIV strain
       RF and contains epitopes that elicit neutralizing antibodies as well as
       T-cell responses. On the basis of 2D proton NMR spectra (COSY, TOCSY,
       and NOESY) of the peptide in aqueous solution, the resonances of nearly
       all hydrogens are assigned. The peptide is largely disordered, but
       specific medium-range NOEs demonstrate conformational preferences in
       certain regions. Part of the N-terminal segment exhibits nascent helical
       conformation, consistent with a finding that many T-cell antigens can be
       modeled as amphipathic helices. In the V3-derived segment of the
       peptide, one region shows evidence of a tight turn conformation,
       corresponding to a turn found previously in V3 peptides of HIV strains
       MN and IIIB. Other conformational features are also detected in the V3
       region, such as a stretch of beta strand and a kink that may arise from
       side-chain interactions.
 DE    Amino Acid Sequence  Antigenic Determinants/*CHEMISTRY  Cross-Linking
       Reagents  Disulfides/CHEMISTRY  HIV/*CHEMISTRY/IMMUNOLOGY  HIV Envelope
       Protein gp120/*CHEMISTRY/IMMUNOLOGY  Molecular Sequence Data  Nuclear
       Magnetic Resonance  Peptides/*CHEMISTRY  Protein Conformation
       Recombinant Fusion Proteins/CHEMISTRY  Support, Non-U.S. Gov't  Support,
       U.S. Gov't, Non-P.H.S.  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).