Synthesis and characterization of the human CC chemokine HCC-2.
J Pept Res
; 54(6): 505-13, 1999 Dec.
Article
en En
| MEDLINE
| ID: mdl-10604595
ABSTRACT
Human CC chemokine 2 (HCC-2) is a novel member of the chemokine peptide family that induces chemotaxis of monocytes, T lymphocytes and eosinophils via activation of the CCR-1 and CCR-3 receptors. Fmoc chemistry was optimized and used to synthesize the biologically active 66-residue peptide HCC-2-(48-113). Introduction of the three disulfide bonds was achieved by oxidative folding in the presence of the redox system cysteine/cystine. Alternatively, a semiselective approach utilizing a mixed Acm/Trt protection scheme for disulfide formation was applied. It was found that, without participation of the two HCC-2-specific cysteine residues in positions 64 and 104, the two typical chemokine disulfides are formed predominantly during oxidative folding. In addition, the mutant [Ala64,104]HCC-2-(48-113) lacking the third disulfide bond that discriminates HCC-2 from most other chemokines was synthesized. For disulfide bond formation, oxidative folding was compared with the use of Acm/Trt protection. HCC-2-(48-113) and the mutant [Ala64,104]HCC-2-(48-113) were further analyzed by CD and one-dimensional 1H NMR-spectroscopy. Both peptides adopt a similar stable secondary and tertiary structure in solution.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Monocinas
/
Quimiocinas CC
Límite:
Humans
Idioma:
En
Revista:
J Pept Res
Asunto de la revista:
BIOQUIMICA
Año:
1999
Tipo del documento:
Article
País de afiliación:
Alemania