Molecular recognition of aqueous dipeptides at multiple hydrogen-bonding sites of mixed peptide monolayers

被引:119
作者
Cha, X
Ariga, K
Kunitake, T
机构
[1] RES DEV CORP JAPAN,SUPERMOL PROJECT,KURUME,FUKUOKA 839,JAPAN
[2] SICHUAN TUMOR INST & HOSP,DEPT BIOL,SO TRAIN STN,CHENGDU 610041,PEOPLES R CHINA
[3] KYUSHU UNIV,FAC ENGN,FUKUOKA 812,JAPAN
关键词
D O I
10.1021/ja961526f
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Oligopeptide amphiphiles with different dipeptide moieties of -XYNH(2) (X = Gly and Ala, Y = Gly, Ala, Val, Leu, and Phe) were synthesized. Binding of aqueous dipeptides onto monolayers of equimolar mixtures of these amphiphiles with a benzoic acid amphiphile (2C(18)BCOOH) was investigated by pi-A isotherm measurement, FT-IR spectroscopy, and XPS elemental analysis. For given GlyX dipeptides (X = neutral and hydrophobic residues), the binding ratio was lessened with increasing sizes of the side chain of the Y residue in the GlyY dipeptide moiety of the host amphiphiles. The Langmuir-type saturation behavior was observed for binding of GlyLeu to an equimolar monolayer of 2C(18)BGly(2)NH(2) and 2C(18)BCOOH. Its binding constant of 475 M(-1) was 10 times larger than that observed for a single-component monolayer of 2C(18)BGly(2)NH(2) (K = 35 M(-1)). The saturation guest/host ratio was 0.47. The mode of substrate insertion into the binding site was examined by FT-IR spectroscopy. When the hydrophobic residue was on the C-terminal of a guest dipeptide (GlyX), the C-terminal insertion was selected with accompanying formation of cyclic carboxylic acid dimers at the interface. In the case of XGly guests, the N-terminal insertion with salt bridge formation with the host was observed. When the two residues of a dipeptide had close hydrophobicities, both C- and N-terminal insertions were observed. Formation of these binding sites is apparently induced by dipeptide binding.
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页码:9545 / 9551
页数:7
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