Interaction of DDSDEEN peptide with N-CAM protein. Possible mechanism enhancing neuronal differentiation.

Abstract:

:DDSDEEN chromatin peptide, after dansylation, was studied for its ability to bind N-CAM protein. The binding causes a quenching of the Dns-peptide fluorescence emission. Dose- and time-dependent binding of Dns-peptide with N-CAM has been shown. Fluorescence quenching is completely lost if the Dns-peptide is subjected to carboxypeptidase digestion. Moreover the undansylated peptide pEDDSDEEN competes with the DnsDDSDEEN peptide for the binding with the N-CAM protein. The Dns-peptide-N-CAM bond has been related to the peptide biological activity probably involved in the promotion of neuronal differentiation. An attempt to recognize a possible N-CAM binding site for Dns-peptide was performed by alignment of N-CAM from various sources with some sequences that have been previously reported as binding sites for the pEDDSDEEN and DDSDEEN peptides. Interestingly, the alignment of N-CAM from various sources with the peptides WHPREGWAL and WFPRWAGQA recognizes on rat and human N-CAM a unique sequence that could be the specific binding site for chromatin peptide: WHSKWYDAK. This sequence is present in fibronectin type-III domain of N-CAM. In addition molecular modeling studies indicate the N-CAM sequence WHSKWYDAK as, probably, the main active site for DnsDDSDEEN (or pEDDSDEEN) peptide ligand. Accordingly the binding experiments show a high affinity between WHSKWYDAK and DnsDDSDEEN peptides.

journal_name

Peptides

journal_title

Peptides

authors

Marsili V,Lupidi G,Berellini G,Calzuola I,Perni S,Cruciani G,Gianfranceschi GL

doi

10.1016/j.peptides.2008.09.008

subject

Has Abstract

pub_date

2008-12-01 00:00:00

pages

2232-42

issue

12

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(08)00396-3

journal_volume

29

pub_type

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