تعيين تتالي النهاية الأمينية و خصائص الببتيد 14 كيلودالتون الملئم للجروح و المعزول من جلد الضفدع Rana esculenta

Abstract EN

Our previous studies have demonstrated the significance of the 14 KDa peptide, isolated from the skin of Rana esculenta in wound healing on animal models and human.

We purified this peptide by a 2 steps protocol involving ion-exchange chromatography and gel filtration, and we separated the 14 KDa doublet band by SDS–PAGE analysis on 17% gel.

In order to identify the 14 KDa, the N-terminal amino acid sequence of 50 amino acids was determined in this study by automated Edman degradation.

The sequence was the following: VHLTDQELKSMNAIWSKVDDKHIGGEALARLLIVYPWTTQYFSSANNNAA.

Extensive homology search for this sequence from the protein data banks using local alignment tool BLAST showed a major N-terminal amino acid sequence similarity with the members of the globin superfamily (52-74%) known to modulate the wound healing process, which explain the great effect of 14 KDa peptide in this process.

In addition, we have sequenced the N-terminal of 10 amino acids of the doublet band of 14 KDa by automated Edman degradation.

Both bands produced an identical N-terminal sequence (VHLTDQELKS).

In this study, we report the identification of a new wound healing peptide in amphibians, which have unique primary structure, which can be classify as a member of the globin superfamily, and we are currently investigating other pharmacological activities of peptides from the skin of R.

esculenta which would be useful in designing peptides for therapeutic applications.