Future medicinal chemistry · 2014
The role of disulfide bonds in structure and activity of chlorotoxin.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Ojeda Paola G, Chan Lai Y, Poth Aaron G, Wang Conan K, Craik David J
Аннотация
BACKGROUND: Chlorotoxin is a small scorpion peptide that inhibits glioma cell migration. We investigated the importance of a major component of chlorotoxin's chemical structure - four disulfide bonds - to its tertiary structure and biological function.
RESULTS: Five disulfide bond analogs of chlorotoxin were synthesized, with l-α-aminobutyric acid residues replacing each or all of the disulfide bonds. Chemical oxidation and circular dichroism experiments revealed that Cys III-VII and Cys V-VIII were essential for native structure formation. Cys I-IV and Cys II-VI were important for stability of enzymatic proteolysis but not for the inhibition of human umbilical vein endothelial cell migration.
CONCLUSION: The disulfide bonds of chlorotoxin are important for its structure and stability and have a minor role in its activity against cell migration.
RESULTS: Five disulfide bond analogs of chlorotoxin were synthesized, with l-α-aminobutyric acid residues replacing each or all of the disulfide bonds. Chemical oxidation and circular dichroism experiments revealed that Cys III-VII and Cys V-VIII were essential for native structure formation. Cys I-IV and Cys II-VI were important for stability of enzymatic proteolysis but not for the inhibition of human umbilical vein endothelial cell migration.
CONCLUSION: The disulfide bonds of chlorotoxin are important for its structure and stability and have a minor role in its activity against cell migration.