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.
Peng
Juan
J
Department of Chemistry, Beijing Normal University, Beijing 100875, P R China.
Zu
Lily
L
Fang
Weihai
W
Huang
Lingyun
L
Wang
Yaru
Y
He
Dacheng
D
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