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Rejection by Neocarzinostatin Protein through Charges Rather than Sizes
Author(s) -
Chin DerHang
Publication year - 1999
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/(sici)1521-3765(19990301)5:3<1084::aid-chem1084>3.0.co;2-k
Subject(s) - thiol , neocarzinostatin , chromophore , chemistry , prodrug , biophysics , mechanism (biology) , biochemistry , combinatorial chemistry , stereochemistry , dna , photochemistry , biology , physics , quantum mechanics
The long‐standing and puzzling selective and protective mechanism of the apoprotein of neocarzinostatin has been clarified by a thiol‐screening test. The ionized acidic amino acid residues repel the negatively charged thiol from attacking the chromophore (depicted). In contrast to what one would generally predict from the lock‐and‐key model, size or shape of the protein does not have a major effect during the actions of the chromoprotein. The data help to explain how the drug activity can be preserved by shielding the chromophore from the attack of the most abundant cellular thiol before the drug reaches the target DNA.