Selective cleavage of protonated penetratin and its substitutes under low-energy collision-induced dissociation condition.
An understanding of the dissociation of penetratin is important for improving its metabolic stability and cargo-delivery efficiency. In this study, we describe the selective cleavage of the K15-K16 amide bond of penetratin under the low-energy collision-induced dissociation condition in mass spectrometry. A variety of penetratin substitutes have been studied in which key basic amino acids have been substituted within the sequence. The calculated structure indicates that an alpha-helix structure prevents the fragmentation of the central peptide domain and the side chain of lysine is involved in the proton translocation process.
Department of Chemistry, Beijing Normal University, Beijing 100875, P R China.
Juan
J
Peng
Lily
L
Zu
Weihai
W
Fang
Lingyun
L
Huang
Yaru
Y
Wang
Dacheng
D
He
D000595:Amino Acid Sequence; D024361:Amino Acids, Basic / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry*; D057846:Cell-Penetrating Peptides; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*
D024361:Amino Acids, Basic; D002352:Carrier Proteins; D057846:Cell-Penetrating Peptides; D010446:Peptide Fragments; C414409:penetratin