DNA-Interactive Properties of Crotamine, a Cell-Penetrating Polypeptide and a Potential Drug Carrier 英文参考文献.docVIP

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DNA-Interactive Properties of Crotamine, a Cell-Penetrating Polypeptide and a Potential Drug Carrier 英文参考文献.doc

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DNA-Interactive Properties of Crotamine, a Cell-Penetrating Polypeptide and a Potential Drug Carrier 英文参考文献

DNA-InteractivePropertiesofCrotamine,aCell- PenetratingPolypeptideandaPotentialDrugCarrier Pei-ChunChen1,MirianA.F.Hayashi2,EduardoBrandtOliveira3,RichardL.Karpel1* 1Department of Chemistry and Biochemistry, University of Maryland Baltimore County (UMBC), Baltimore, Maryland, United States of America, 2Departamento de Farmacologia, Universidade Federal de Sa?o Paulo (UNIFESP), Sa?o Paulo, Sa?o Paulo, Brazil, 3Departamento de Bioqu?′mica e Imunologia, Faculdade de Medicina, UniversidadedeSa?o Paulo(USP),Ribeira?o Preto,Brazil Abstract Crotamine,a42-residuepolypeptidederivedfromthevenomoftheSouthAmericanrattlesnakeCrotalusdurissusterrificus, has been shown to be a cell-penetrating protein that targets chromosomes, carries plasmid DNA into cells, and shows specificityforactivelyproliferatingcells.Giventhispotentialroleasanucleicacid-deliveryvector,wehavestudiedindetail thebindingofcrotaminetosingle-anddouble-strandedDNAsofdifferentlengthsandbasecompositionsoverarangeof ionic conditions. Agarose gel electrophoresis and ultraviolet spectrophotometry analysis indicate that complexes of crotaminewithlong-chainDNAsreadilyaggregateandprecipitateatlowionicstrength.Thisaggregation,whichmaybe importantforcellularuptakeofDNA,becomeslesslikelywithshorterchainlength.25-meroligonucleotidesdonotshow any evidence of such aggregation, permitting the determination of affinities and size via fluorescence quenching experiments. The polypeptide binds non-cooperatively to DNA, covering about 5 nucleotide residues when it binds to single(ss)or(ds)doublestrandedmolecules.Theaffinitiesoftheproteinforss-vs.ds-DNAarecomparable,andinversely proportionaltosaltlevels.Analysisofthedependenceofaffinityon[NaCl]indicatesthatthereareamaximumof, 3ionic interactions between the protein and DNA, with some of the binding affinity attributable to non-ionic interactions. Inspection of the three-dimensional structure of the protein suggests that residues 31 to 35, Arg-Trp-Arg-Trp-Lys, could serveasapotent