title: In vitro stability of alpha-helical peptide nucleic acids (alphaPNAs).
abstract: Alpha-helical peptide nucleic acids (alphaPNAs) are synthetic molecules that merge the alpha-helix secondary structure of peptides with the codified Watson-Crick base pairing capability of nucleic acids. It is now demonstrated that alphaPNAs made up of either L- or D-amino acids are resistant to degradation by the proteases present in human serum. The increased stability of alphaPNAs towards proteases may be attributable to the presence of unnatural nucleoamino acid residues [-NHCH(CH(2)OCH(2)B)CO-, where B=thymine or cytosine] since the replacement of these amino acids by serine yields a control peptide that does break down in human serum. The stability of alphaPNAs towards proteases makes them attractive candidates for further development as antisense agents.
authors.affiliation: Department of Chemistry, Case Western Reserve University, Cleveland, OH 44106-7078, USA. ppg@po.cwru.edu
authors.forename: P
authors.initials: P
authors.lastname: Garner
authors.forename: B
authors.initials: B
authors.lastname: Sherry
authors.forename: S
authors.initials: S
authors.lastname: Moilanen
authors.forename: Y
authors.initials: Y
authors.lastname: Huang
mesh_terms: D000595:Amino Acid Sequence; D001769:Blood / Q000378:metabolism; D004355:Drug Stability; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D020135:Peptide Nucleic Acids / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D020135:Peptide Nucleic Acids; D010450:Endopeptidases