Arnon R, Maron E, Sela M, Anfinsen C B
Proc Natl Acad Sci U S A. 1971 Jul;68(7):1450-5. doi: 10.1073/pnas.68.7.1450.
A synthetic peptide consisting of the aminoacid sequence of residues 64-82 of lysozyme, with alanine replacing cysteine as residue 76, was prepared by the solid-phase technique. Mild reduction followed by reoxidation in air of the deprotected peptide led to the formation of a closed loop containing an intrachain disulfide bond. A conjugate consisting of this "loop" attached to multi-poly(DL-alanyl)-poly(L-lysine) elicited, in rabbits and goats, the formation of antibodies capable of reacting with lysozyme and with the loop peptide prepared from it. These immunological interactions can be inhibited by either lysozyme or the loop peptide, but not by the performic acid-oxidized open-chain peptide. Thus, the antibodies elicited by the completely synthetic antigen show specificity toward the "loop" structure (residues 64-80) of native lysozyme.
通过固相技术制备了一种合成肽,其氨基酸序列为溶菌酶64 - 82位残基,其中76位残基的半胱氨酸被丙氨酸取代。对脱保护的肽进行温和还原,然后在空气中再氧化,导致形成一个含有链内二硫键的闭环。由这种“环”与多聚(DL - 丙氨酰)- 聚(L - 赖氨酸)连接而成的缀合物,在兔和山羊体内引发了能够与溶菌酶以及由其制备的环肽发生反应的抗体的形成。这些免疫相互作用可被溶菌酶或环肽抑制,但不能被过甲酸氧化的开链肽抑制。因此,由完全合成抗原引发的抗体对天然溶菌酶的“环”结构(64 - 80位残基)具有特异性。