Kissper, a kiwi fruit peptide with channel-like activity: structural and functional features.
Kissper is a 39-residue peptide isolated from kiwi fruit (Actinidia deliciosa). Its primary structure, elucidated by direct protein sequencing, is identical to the N-terminal region of kiwellin, a recently reported kiwi fruit allergenic protein, suggesting that kissper derives from the in vivo processing of kiwellin. The peptide does not show high sequence identity with any other polypeptide of known function. However, it displays a pattern of cysteines similar, but not identical, to those observed in some plant and animal proteins, including toxins involved in defence mechanisms. A number of these proteins are also active on mammalian cells. Functional characterization of kissper showed pH-dependent and voltage-gated pore-forming activity, together with anion selectivity and channeling in model synthetic PLMs, made up of POPC and of DOPS:DOPE:POPC. A 2DNMR analysis indicates that in aqueous solution kissper has only short regions of regular secondary structure, without any evident similarity with other bioactive peptides. Comparative analysis of the structural and functional features suggests that kissper is a member of a new class of pore-forming peptides with potential effects on human health.
Ciardiello
M Antonietta
MA
Istituto di Biochimica delle Proteine, CNR, Napoli, Italy. ma.ciardiello@ibp.cnr.it
Meleleo
Daniela
D
Saviano
Gabriella
G
Crescenzo
Roberta
R
Carratore
Vito
V
Camardella
Laura
L
Gallucci
Enrico
E
Micelli
Silvia
S
Tancredi
Teodorico
T
Picone
Delia
D
Tamburrini
Maurizio
M
D029042:Actinidia / Q000737:chemistry*; D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D010940:Plant Proteins