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首页> 外文期刊>Journal of the American Chemical Society >MOLECULAR RECOGNITION OF AQUEOUS DIPEPTIDES AT MULTIPLE HYDROGEN-BONDING SITES OF MIXED PEPTIDE MONOLAYERS
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MOLECULAR RECOGNITION OF AQUEOUS DIPEPTIDES AT MULTIPLE HYDROGEN-BONDING SITES OF MIXED PEPTIDE MONOLAYERS

机译：混合多肽单分子在多个氢键处的多肽的分子识别

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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.
机译：合成了具有-XYNH（2）不同二肽部分的寡肽两亲物（X = Gly和Ala，Y = Gly，Ala，Val，Leu和Phe）。通过pi-A等温线测量，FT-IR光谱和XPS元素分析研究了二肽水溶液与这些两亲物与苯甲酸两亲物（2C（18）BCOOH）的等摩尔混合物的单层结合。对于给定的GlyX二肽（X =中性和疏水残基），随着宿主两亲物GlyY二肽部分中Y残基侧链尺寸的增加，结合率降低。观察到的Langmuir型饱和行为可将GlyLeu与2C（18）BGly（2）NH（2）和2C（18）BCOOH的等摩尔单分子层结合。它的结合常数为475 M（-1），比2C（18）BGly（2）NH（2）的单组分单层所观察到的结合常数大10倍（K = 35 M（-1））。饱和宾客/主人比为0.47。通过FT-IR光谱检查底物插入结合位点的方式。当疏水残基位于客体二肽（GlyX）的C末端时，选择C末端插入并伴随在界面处形成环状羧酸二聚体。在XGly客体的情况下，观察到与宿主形成盐桥的N末端插入。当二肽的两个残基具有紧密的疏水性时，观察到C-和N-末端插入。这些结合位点的形成显然是由二肽结合诱导的。

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