SPONTANEOUS ASSEMBLY OF A SELF-COMPLEMENTARY OLIGOPEPTIDE TO FORM A STABLE MACROSCOPIC MEMBRANE

被引:1065
作者
ZHANG, SG
HOLMES, T
LOCKSHIN, C
RICH, A
机构
[1] MIT, DEPT BIOL 16-739, CAMBRIDGE, MA 02139 USA
[2] MIT, DEPT BRAIN & COGNIT SCI, CAMBRIDGE, MA 02139 USA
关键词
BETA-SHEET; INSOLUBLE FILAMENTS; IONIC BONDS; ORIGIN OF LIFE; ZUOTIN;
D O I
10.1073/pnas.90.8.3334
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
A 16-residue peptide [(Ala-Glu-Ala-Glu-Ala-Lys-Ala-Lys)2] has a characteristic beta-sheet circular dichroism spectrum in water. Upon the addition of salt, the peptide spontaneously assembles to form a macroscopic membrane. The membrane does not dissolve in heat or in acidic or alkaline solutions, nor does it dissolve upon addition of guanidine hydrochloride, SDS/urea, or a variety of proteolytic enzymes. Scanning EM reveals a network of interwoven filaments almost-equal-to 10-20 nm in diameter. An important component of the stability is probably due to formation of complementary ionic bonds between glutamic and lysine side chains. This phenomenon may be a model for studying the insoluble peptides found in certain neurological disorders. It may also have implications for biomaterials and origin-of-life research.
引用
收藏
页码:3334 / 3338
页数:5
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