Peptides are amino acid polymers. They are generally much smaller than proteins and don’t have sufficient activity on their own – they generally represent a small portion of a full protein. They may also be signalling molecules that act through interaction with specific receptors, as in peptide hormones and cytokines.

Latest Research and Reviews

News and Comment

  • News and Views |

    Despite their potential as drugs, peptides are generally not cell permeable, which limits their practical applications in medicine. Now, linear peptides have been cyclized by using a heteroaromatic linker. This cyclization both improves passive membrane permeability and stabilizes a biologically relevant secondary structure.

    • Fumito Saito
    •  & Jeffrey W. Bode
    Nature Chemistry 8, 1085–1086
  • News and Views |

    A potent toxin present in the venom of a fish-hunting cone snail is a minimized insulin (Con-Ins G1) lacking key residues involved in the receptor binding of most insulins. New data show that Con-Ins G1 nevertheless binds potently to the human insulin receptor, owing to a rearrangement that compensates for the lack of a critical binding residue.

    • Pierre De Meyts
  • News and Views |

    Stapled helices are promising compounds for inhibiting intracellular protein–protein interactions, but the discovery of peptides with the key property of cellular uptake has taken place largely through trial and error. A new study defines physicochemical parameters for designing hydrocarbon-stapled helices with a greater likelihood of cellular uptake.

    • Joshua A Kritzer
  • News and Views |

    An artificial esterase with no known natural structural analogues has been formed via the homo-heptameric self-assembly of a designed peptide. This esterase represents the first report of a functional catalytic triad rationally engineered into a de novo protein framework.

    • Olga V. Makhlynets
    •  & Ivan V. Korendovych
    Nature Chemistry 8, 823–824