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Oxidative folding of nerve growth factor can be mediated by the pro‐peptide of neurotrophin‐3
Author(s) -
Hauburger Anja,
Kliemannel Marco,
Madsen Peder,
Rudolph Rainer,
Schwarz Elisabeth
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.063
Subject(s) - nerve growth factor , peptide , chemistry , neurotrophin , oxidative phosphorylation , fusion protein , biochemistry , oxidative folding , microbiology and biotechnology , biology , recombinant dna , receptor , cysteine , enzyme , gene
We have previously shown that the pro‐peptide of human nerve growth factor (NGF) facilitates oxidative folding of the mature part. For the analysis of functional specificities of the pro‐peptides of NGF and the related neurotrophin‐3 (NT‐3) with respect to structure formation, chimeric proteins with swapped pro‐peptides were generated. Neither the structure nor the stability of the mature domains was influenced by the heterologous pro‐peptides. For the pro‐peptide of NT‐3 fused to the mature part of NGF, stabilization of the pro‐peptide moiety by the NGF part was observed. Folding kinetics and renaturation yields of this chimeric protein were comparable to those of proNGF. Our results demonstrate functional interchangeability between the pro‐peptides of NGF and NT‐3 with respect to their role in assisting oxidative folding of the mature part.