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Design, synthesis, and conformational studies of the hGM-CSF derived peptide (13–27)–Gly–(75–87) by E. Peggion; S. Mammi; E. Schievano; R. P. Revoltella; C. Galoppini; P. Rovero is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Design, synthesis, and conformational studies of the hGM-CSF derived peptide (13–27)–Gly–(75–87) about?

An analogue of the human granulocyte-macrophage colony-stimulating factor (hGM-CSF), hGM-CSF (13-27)-Gly-(75-87) was synthesized by solid phase methodology. This analogue was designed to comprise helices A and C of the native growth factor, linked by a glycine bridge. Helices A and C form half of a four-helix bundle motif in the crystal structure of the native factor and are involved in the interaction with ␣and ␤-chains of the heterodimeric receptor. A conformational analysis of the synthetic analogue by CD, two-dimensional nmr spectroscopy, and molecular dynamics calculations is reported. The analogue is in a random structure in water and assumes a partially ␣-helical conformation in a 1 : 1 trifluoroethanol/water mixture. The helix content in this medium is ϳ 70%. By 2D-nmr spectroscopy, two helical segments were identified in the sequences corresponding to helices A and C. In addition to medium-and short-range NOESY connectivities, a long-range cross peak was found between the C␤ proton of Val 16 and NH proton of His 87 (using the numbering of the native protein). Experimentally derived interproton distances were used as restraints in molecular dynamics calculations, utilizing

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Author

E. Peggion; S. Mammi; E. Schievano; R. P. Revoltella; C. Galoppini; P. Rovero

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)