title: Controlling the Helix Handedness of ααβ-Peptide Foldamers through Sequence Shifting.
abstract: Peptide foldamers containing both cis-β-aminocyclopentanecarboxylic acid and α-amino acid residues combined in various sequence patterns (ααβ, αααβ, αβααβ, and ααβαααβ) were screened using CD and NMR spectroscopy for the tendency to form helices. ααβ-Peptides were found to fold into an unprecedented and well-defined 16/17/15/18/14/17-helix. By extending the length of the sequence or shifting a fragment of the sequence from one terminus to another in ααβ-peptides, the balance between left-handed and right-handed helix populations present in the solution can be controlled. Engineering of the peptide sequence could lead to compounds with either a strong propensity for the selected helix sense or a mixture of helical conformations of opposite senses.
authors.affiliation: Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
authors.forename: Monika
authors.initials: M
authors.lastname: Szefczyk
authors.affiliation: Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
authors.forename: Ewelina
authors.initials: E
authors.lastname: Węglarz-Tomczak
authors.affiliation: Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
authors.forename: Paulina
authors.initials: P
authors.lastname: Fortuna
authors.affiliation: Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Krzysztoń
authors.affiliation: Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
authors.forename: Ewa
authors.initials: E
authors.lastname: Rudzińska-Szostak
authors.affiliation: Department of Bioorganic Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370, Wrocław, Poland.
authors.forename: Łukasz
authors.identifier: 0000-0003-0318-4944
authors.initials: Ł
authors.lastname: Berlicki
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D002942:Circular Dichroism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids; D010455:Peptides
keywords: foldamers; helical propensity; peptide structures; peptides; β-amino acids