The Structural Requirements for an Inverse Substrate for Enzymatic Peptide Synthesis: Position Isomers of Guanidinonaphthyl Esters as the Acyl Donor Component.
The Structural Requirements for an Inverse Substrate for Enzymatic Peptide Synthesis: Position Isomers of Guanidinonaphthyl Esters as the Acyl Donor Component.
复制标题
酶促肽合成的反向底物的结构要求：作为酰基供体组分的胍基萘酯的位置异构体。
DOI：
10.1248/cpb.47.104
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发表时间：
1999
影响因子：
1.7
通讯作者：
K. Tanizawa
中科院分区：
文献类型：
--
作者：
H. Sekizaki;K. Itoh;E. Toyota;K. Tanizawa
制备了四种N-叔丁氧羰基氨基酸衍生的胍基萘酯的位置异构体作为胰蛋白酶催化肽合成的酰基供体组分。分析了这些合成的逆底物对自发水解和胰蛋白酶水解的动力学行为。发现这些底物很容易与α-氨基酸对硝基苯胺偶联生成肽。4-胍基-1-萘基酯，其中胍基和羰基在萘环的短轴上线性排列，是酶促肽合成的最有效底物。该方法特别适用于含α，α-二烷基氨基酸的多肽的制备。所得产物的酶促水解可忽略不计。
Four series of inverse substrates, position isomers of guanidinonaphthyl esters derived from N-(tert-butyloxycarbonyl)amino acid, were prepared as acyl donor components for trypsin-catalyzed peptide synthesis. The kinetic behavior of these synthetic inverse substrates toward spontaneous and tryptic hydrolysis was analyzed. These substrates were found to readily couple with α-amino acid p-nitroanilide to produce peptide. 4-Guanidino-1-naphthyl esters, in which the guanidino group and the carbonyl group are aligned linearly on the shorter axis of the naphthalene ring, were the most efficient substrates for enzymatic peptide synthesis. The method was especially useful for the preparation of peptides containing α, α-dialkyl amino acids. The enzymatic hydrolysis of the resulting products was negligible.