TY - JOUR
T1 - Functional analysis of synthetic substructures of polytheonamide B
T2 - A transmembrane channel-forming peptide
AU - Matsuoka, Shigeru
AU - Shinohara, Naoki
AU - Takahashi, Tomoaki
AU - Iida, Maiko
AU - Inoue, Masayuki
PY - 2011/5/16
Y1 - 2011/5/16
N2 - Longer is better: PolytheonamideB, the largest nonribosomal linear peptide identified to date, is a transmembrane channel-forming peptide. Nine of its substructures have now been chemically synthesized. The membrane-disrupting and ion-channel-forming sequences as well as the cytotoxicity-enhancing sequence have been identified.
AB - Longer is better: PolytheonamideB, the largest nonribosomal linear peptide identified to date, is a transmembrane channel-forming peptide. Nine of its substructures have now been chemically synthesized. The membrane-disrupting and ion-channel-forming sequences as well as the cytotoxicity-enhancing sequence have been identified.
KW - biological activity
KW - ion channels
KW - natural products
KW - nonribosomal peptides
KW - structure-activity relationships
UR - http://www.scopus.com/inward/record.url?scp=79955785158&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79955785158&partnerID=8YFLogxK
U2 - 10.1002/anie.201101533
DO - 10.1002/anie.201101533
M3 - Article
C2 - 21520376
AN - SCOPUS:79955785158
SN - 1433-7851
VL - 50
SP - 4879
EP - 4883
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 21
ER -