Immunogenic peptides corresponding to the dominant antigenic region alanine-597 to cysteine-619 in the transmembrane protein of simian immunodeficiency virus have a propensity to fold in aqueous solution
Two synthetic peptides corresponding to the N- and C-terminal halves of a 23 amino acid sequence representing an immunodominant domain of the simian immunodeficiency virus of macaque origin (SIVmac) were examined for conformational preferences in aqueous solution by proton nuclear magnetic resonance...
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Published in | Biochemistry (Easton) Vol. 31; no. 5; pp. 1458 - 1463 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
11.02.1992
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Subjects | |
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Abstract | Two synthetic peptides corresponding to the N- and C-terminal halves of a 23 amino acid sequence representing an immunodominant domain of the simian immunodeficiency virus of macaque origin (SIVmac) were examined for conformational preferences in aqueous solution by proton nuclear magnetic resonance methods. The two constituent peptides, termed A12-7 (Ala597-Ile-Glu-Lys-Tyr-Leu-Glu-Asp-Gln-Ala-Gln607) and A12-9 (Leu608-Asn-Ala-Trp-Gly-Cys-Ala-Phe-Arg-Gln-Val-Ser619), were found to contain a considerable conformational preference for states in which the backbone phi and psi angles populate the alpha region of the Ramachandran plot. Further, for peptide A12-9, the types and intensities of the nuclear Overhauser effect (NOE) connectivities between protons in the polypeptide backbone suggest that these states appear to include helical turns. The temperature dependence of the amide proton chemical shifts indicates that some degree of intramolecular hydrogen bonding occurs in these peptides. These results are consistent with a model in which immunogenic peptides which induce antibodies reactive with the intact protein from which the peptide sequence was derived contain conformational preferences in water solution for states other than the extended-chain forms typically found in "random coil" peptides. |
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AbstractList | Two synthetic peptides corresponding to the N- and C-terminal halves of a 23 amino acid sequence representing an immunodominant domain of the simian immunodeficiency virus of macaque origin (SIVmac) were examined for conformational preferences in aqueous solution by proton nuclear magnetic resonance methods. The two constituent peptides, termed A12-7 (Ala597-Ile-Glu-Lys-Tyr-Leu-Glu-Asp-Gln-Ala-Gln607) and A12-9 (Leu608-Asn-Ala-Trp-Gly-Cys-Ala-Phe-Arg-Gln-Val-Ser619), were found to contain a considerable conformational preference for states in which the backbone phi and psi angles populate the alpha region of the Ramachandran plot. Further, for peptide A12-9, the types and intensities of the nuclear Overhauser effect (NOE) connectivities between protons in the polypeptide backbone suggest that these states appear to include helical turns. The temperature dependence of the amide proton chemical shifts indicates that some degree of intramolecular hydrogen bonding occurs in these peptides. These results are consistent with a model in which immunogenic peptides which induce antibodies reactive with the intact protein from which the peptide sequence was derived contain conformational preferences in water solution for states other than the extended-chain forms typically found in "random coil" peptides. Two synthetic peptides corresponding to the N- and C-terminal halves of a 23 amino acid sequence representing an immunodominant domain of the simian immunodeficiency virus of macaque origin (SIV sub(mac)) were examined for conformational preferences in aqueous solution by proton nuclear magnetic resonance methods. |
Author | Lerner, Richard A Norrby, Erling Hoey, Kenway Parks, D. Elliot Wright, Peter E Dyson, H. Jane |
Author_xml | – sequence: 1 givenname: H. Jane surname: Dyson fullname: Dyson, H. Jane – sequence: 2 givenname: Erling surname: Norrby fullname: Norrby, Erling – sequence: 3 givenname: Kenway surname: Hoey fullname: Hoey, Kenway – sequence: 4 givenname: D. Elliot surname: Parks fullname: Parks, D. Elliot – sequence: 5 givenname: Richard A surname: Lerner fullname: Lerner, Richard A – sequence: 6 givenname: Peter E surname: Wright fullname: Wright, Peter E |
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Keywords | Virus Antigen Transmembrane protein Synthetic product Peptides Retroviridae Lentivirinae NMR spectrometry Simian immunodeficiency virus Conformation |
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SubjectTerms | AIDS/HIV alanine Alanine - chemistry Alanine - immunology Amino Acid Sequence Animals Antibody Specificity Antigenic determinants, haptens, artificial antigens Antigens Biological and medical sciences Cross Reactions cysteine Cysteine - chemistry Cysteine - immunology Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunodominant Epitopes - chemistry Immunodominant Epitopes - immunology Macaca Magnetic Resonance Spectroscopy Mice Molecular immunology Molecular Sequence Data Peptide Fragments - immunology Protein Conformation Rabbits Simian Immunodeficiency Virus - chemistry Simian Immunodeficiency Virus - immunology Solutions Viral Envelope Proteins - chemistry Viral Envelope Proteins - immunology |
Title | Immunogenic peptides corresponding to the dominant antigenic region alanine-597 to cysteine-619 in the transmembrane protein of simian immunodeficiency virus have a propensity to fold in aqueous solution |
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