A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenic peptide.

G Siligardi, A F Drake, P Mascagni, D J Rowlands, F Brown, W A Gibbons
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Abstract

The circular dichroism spectrum of the 20-residue immunogenic peptide from the foot-and-mouth disease virus (VP1; 141-160 of serotype A, subtype 12) was solvent- and temperature-dependent. Careful solvent titration revealed two isodichroic points and plateaux consistent with stepwise unfolding of specific stable conformations. Variable temperature studies in cryogenic solvents and urea perturbation were consistent with the existence of three conformational moieties, the left-handed extended helix, the alpha-helix, and the 3(10) helix. The number of residues in each helix was confirmed by CD spectral simulations. The strategy described here can be used to determine the components of a conformational equilibrium and their statistical weights, to study peptide folding and unfolding and to determine the bioactive conformation(s) of linear peptides. The conclusions were supported by 2D-NMR studies. A new mechanism for the stabilization of left-handed extended helices and destabilization of alpha-helices by urea is proposed. The structure of the peptide as resolved by CD spectroscopy is of particular significance since the conformation of this antigenic sequence in situ has so far not been solved by X-ray crystallography.

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用于多肽折叠/展开研究的CD策略。一种合成的口蹄疫病毒免疫原肽。
口蹄疫病毒(VP1) 20残基免疫原肽的圆二色谱分析血清型A的141-160,亚型12)依赖于溶剂和温度。仔细的溶剂滴定发现了两个等向色点和平台,与特定稳定构象的逐步展开一致。在低温溶剂和尿素扰动下的变温研究证实了三种构象的存在,即左旋扩展螺旋、α -螺旋和3(10)螺旋。通过CD谱模拟确定了每个螺旋中的残基数。这里描述的策略可用于确定构象平衡的组成部分及其统计权重,研究肽折叠和展开,并确定线性肽的生物活性构象。这些结论得到了二维核磁共振研究的支持。提出了左旋扩展螺旋稳定和α -螺旋被尿素破坏的新机制。由于该抗原序列的原位构象迄今尚未由x射线晶体学解决,因此用CD光谱解析的肽的结构具有特别重要的意义。
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