GENERAL-METHOD FOR THE RAPID SOLID-PHASE SYNTHESIS OF LARGE NUMBERS OF PEPTIDES - SPECIFICITY OF ANTIGEN-ANTIBODY INTERACTION AT THE LEVEL OF INDIVIDUAL AMINO-ACIDS
GENERAL-METHOD FOR THE RAPID SOLID-PHASE SYNTHESIS OF LARGE NUMBERS OF PEPTIDES - SPECIFICITY OF ANTIGEN-ANTIBODY INTERACTION AT THE LEVEL OF INDIVIDUAL AMINO-ACIDS
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DOI：
10.1073/pnas.82.15.5131
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
HOUGHTEN, RA
中科院分区：
文献类型：
--
作者：
HOUGHTEN, RA
描述了一种新颖而简单的方法，其促进了大量肽的合成，使得合成过程不再需要成为涉及肽的许多研究中的限制因素。通过使用所述方法，在< 4周内制备并表征了10-20 mg代表流感血凝素蛋白（HA 1）片段的单个氨基酸变体的248种不同的13-残基肽。通过检查这些类似物与针对HA 1残基75-110产生的单克隆抗体的结合，发现单个氨基酸，即位置101处的天冬氨酸，对相互作用具有独特的重要性。另外两个残基，天冬氨酸-104和丙氨酸-106，被发现发挥较小，但显着的作用，在结合相互作用。其他单一位置残基的变化似乎是很少或没有重要性。
A novel yet simple method is described that facilitates the synthesis of large numbers of peptides to the extent that the synthesis process need no longer be the limiting factor in many studies involving peptides. By using the methods described, 10-20 mg of 248 different 13-residue peptides representing single amino acid variants of a segment of the influenza hemagglutinin protein (HA1) have been prepared and characterized in < 4 wk. Through examination of the binding of these analogs to monoclonal antibodies raised against residues 75-110 of HA1, it was found that a single amino acid, aspartic acid at position 101, is of unique importance to the interaction. Two other residues, aspartic acid-104 and alanine-106, were found to play a lesser but significant role in the binding interaction. Other single positional residue variations appear to be of little or no importance.