Abstract:
:The binding of glycosaminoglycans to a synthetic peptide (SKAQKAQAKQAKQAQKAQKAQAKQAKQW-CONH(2)), consisting of a hybrid consensus heparin binding sequence, is studied using circular dichroism, fluorescence anisotropy and nuclear magnetic resonance techniques. The results unveil certain novel features, most importantly, the peptide binds preferentially to iduronic acid containing glycosaminoglycans and the dissociation constant for the peptide-heparin complex was found to be 30 nM. Interestingly, higher order intermolecular association(s)/aggregation was not observed, especially at saturating concentrations of the ligand. The helical structure of the peptide backbone, induced upon binding to a particular glycosaminoglycan is directly related to their binding affinity. In our opinion, studies on such unconventional hybrid peptide sequences containing low density basic amino acid residues would lead to the design of sequence specific glycosaminoglycan binding peptides.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Jayaraman G,Wu CW,Liu YJ,Chien KY,Fang JC,Lyu PCdoi
10.1016/s0014-5793(00)01964-5keywords:
subject
Has Abstractpub_date
2000-09-29 00:00:00pages
154-8issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01964-5journal_volume
482pub_type
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