title: Introduction of a tailor made anion receptor into the side chain of small peptides allows fine-tuning the thermodynamic signature of peptide-DNA binding.
abstract: The binding between peptides and DNA is often driven by entropic forces. We demonstrate herein a new approach to shift the thermodynamic profile of peptide/DNA binding from entropy to enthalpy driven. This eventually leads to higher compacted DNA aggregates which are important for gene transfection.
authors.affiliation: Institute for Organic Chemistry, University of Duisburg-Essen, 45117, Essen, Germany. carsten.schmuck@uni-due.de.
authors.forename: Mao
authors.initials: M
authors.lastname: Li
authors.affiliation: Institute for Biology, University of Duisburg-Essen, 45117, Essen, Germany.
authors.forename: Stefanie
authors.initials: S
authors.lastname: Schlesiger
authors.affiliation: Institute for Biology, University of Duisburg-Essen, 45117, Essen, Germany.
authors.forename: Shirley K
authors.initials: SK
authors.lastname: Knauer
authors.affiliation: Institute for Organic Chemistry, University of Duisburg-Essen, 45117, Essen, Germany. carsten.schmuck@uni-due.de.
authors.forename: Carsten
authors.initials: C
authors.lastname: Schmuck
mesh_terms: D001665:Binding Sites; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019277:Entropy; D006367:HeLa Cells; D006801:Humans; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics; D014162:Transfection / Q000379:methods
chemical_list: D010455:Peptides; D004247:DNA