SELECTION OF PEPTIDE INHIBITORS OF INTERACTIONS INVOLVED IN COMPLEX PROTEIN ASSEMBLIES - ASSOCIATION OF THE CORE AND SURFACE-ANTIGENS OF HEPATITIS-B VIRUS

被引:97
作者
DYSON, MR [1 ]
MURRAY, K [1 ]
机构
[1] UNIV EDINBURGH,INST CELL & MOLEC BIOL,EDINBURGH EH9 3JR,MIDLOTHIAN,SCOTLAND
关键词
PHAGE DISPLAY; PEPTIDE LIBRARIES; MORPHOGENESIS; ANTIVIRAL AGENT;
D O I
10.1073/pnas.92.6.2194
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
As an example for studies of contacts involved in complex biological systems, peptide ligands that bind to the core antigen of hepatitis B virus (HBcAg) have been selected from a random hexapeptide library displayed on filamentous phage. Affinity-purified phage bearing aa seqnence LLGRMK, or some related sequences, bound full-length or truncated HBcAg but did not bind denatured HBcAg. The long (L), but not the short (S), hepatitis B virus envelope polypeptide, when synthesized in an in vitro system, bound firmly to HBcAg, indicating that interaction between HBcAg and the pre-S region of the L polypeptide is critical for virus morphogenesis. This interaction was inhibited by peptide ALLGRMKG, suggesting that this and related small molecules may inhibit viral assembly.
引用
收藏
页码:2194 / 2198
页数:5
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