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Solid‐phase Synthesis of a Peptide Derivative of Thymosin alpha1 and Initial Studies on its 99m Tc‐Radiolabelling
Author(s) -
Klimentzou Persefoni,
Beck Alexander,
Varvarigou Alexandra,
Tsitsilonis Ourania,
Voelter Wolfgang,
Pirmettis Ioannis,
Papadopoulos Minas,
Livaniou Evangelia,
Zikos Christos
Publication year - 2007
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2007.00529.x
Subject(s) - peptide , chemistry , solid phase synthesis , moiety , peptide synthesis , thymosin , cysteine , stereochemistry , residue (chemistry) , bifunctional , derivative (finance) , lysine , pentapeptide repeat , amino acid , combinatorial chemistry , biochemistry , enzyme , financial economics , economics , catalysis
A derivative ( 1 ) of the immunopotentiating 28‐peptide thymosin alpha1 has been especially designed, so that it can be 99m Tc‐radiolabelled, and synthesized following the Fmoc solid‐phase peptide synthesis approach. Derivative 1 contains the N‐terminal fragment T α 1[1‐14] as a bioactive segment, at the C‐terminus of which a 99m Tc‐chelating moiety consisting of N α , N α ‐dimethylglycine, serine and cysteine is linked through the N ɛ ‐amino group of a ‘bifunctional’ lysine residue; the latter is indirectly anchored on the solid‐phase peptide synthesis resin through 6‐aminocaproic acid ( dm GSCK{ N ɛ ‐T α 1[1‐14]}Aca). Synthetic derivative 1 was obtained at high overall yield (approximately 35%) and purity (>95%) and shown to be efficiently radiolabelled with 99m Tc, thus resulting in the first, to our knowledge, so far reported 99m Tc‐radiolabelled derivative of thymosin alpha1, which may be eventually used as a specific molecular tool for the in vitro / in vivo study of the mode of action of the parent bioactive peptide.