Fernández I, Ubach J, Reig F, Andreu D, Pons M
Department de Química Orgànica, Universitat de Barcelona, Spain.
Biopolymers. 1994 Sep;34(9):1251-8. doi: 10.1002/bip.360340913.
A 15-residue hybrid peptide (KWKLFKKIGAVLKVL-amide) incorporating partial sequences of cecropin A and melittin causes the release of carboxyfluoresceine encapsulated in phosphatidylcholine liposomes. Succinylation of the amino groups in the N-terminus and lysine side chains inhibits the effect of this peptide on liposome permeability. Conformational analysis of the parent peptide and its succinyl derivative by CD and nmr indicates that both peptides form amphipathic alpha-helices in the presence of hexafluoro-2-propanol, but only the unmodified peptide acquires a relevant level of alpha-helical conformation in the presence of liposomes.
一种包含天蚕素A和蜂毒素部分序列的15个残基的杂合肽（KWKLFKKIGAVLKVL-酰胺）可导致包裹在磷脂酰胆碱脂质体中的羧基荧光素释放。N端氨基和赖氨酸侧链的琥珀酰化抑制了该肽对脂质体通透性的影响。通过圆二色光谱（CD）和核磁共振（NMR）对亲本肽及其琥珀酰衍生物进行构象分析表明，在六氟-2-丙醇存在下，两种肽均形成两亲性α-螺旋，但只有未修饰的肽在脂质体存在下能获得相关水平的α-螺旋构象。
