Jelicks L A, Broido M S, Becker J M, Naider F R
Department of Chemistry, Hunter College, New York, New York 10021.
Biochemistry. 1989 May 16;28(10):4233-40. doi: 10.1021/bi00436a017.
Proton and phosphorus-31 nuclear magnetic resonance (1H and 31P NMR) studies of the interaction between a tridecapeptide pheromone, the alpha-factor of Saccharomyces cerevisiae, and sonicated lipid vesicles are reported. 31P NMR studies demonstrate that there is interaction of the peptide with the phosphorus headgroups, and quasielastic light scattering (QLS) studies indicate that lipid vesicles increase in size upon addition of peptide. Previous solution (aqueous and DMSO) studies from this laboratory indicate that alpha-factor is highly flexible with only one long-lived identifiable structural feature, a type II beta-turn spanning the central portion of the peptide. Two-dimensional (2D) 1H nuclear Overhauser effect spectroscopy (NOESY) studies demonstrate a marked ordering of the peptide upon interaction with lipid, suggesting a compact N-terminus, in addition to a stabilized beta-turn. In contrast to our results in both solution and lipid environment, Wakamatsu et al. [Wakamatsu, K., Okada, A., Suzuki, M., Higashijima, T., Masui, Y., Sakakibara, S., & Miyazawa, T. (1986) Eur. J. Biochem. 154, 607-615] proposed a lipid environment conformation, on the basis of one-dimensional transferred NOE studies in D2O, which does not include the beta-turn.
本文报道了对十三肽信息素（酿酒酵母α因子）与超声处理的脂质囊泡之间相互作用的质子和磷-31核磁共振（1H和31P NMR）研究。31P NMR研究表明该肽与磷头部基团存在相互作用，准弹性光散射（QLS）研究表明添加肽后脂质囊泡尺寸增大。本实验室之前的溶液（水相和二甲基亚砜）研究表明，α因子具有高度的灵活性，只有一个长寿命的可识别结构特征，即跨越肽中央部分的II型β-转角。二维（2D）1H核Overhauser效应光谱（NOESY）研究表明，该肽与脂质相互作用后呈现出显著的有序性，这表明除了稳定的β-转角外，还有一个紧密的N端。与我们在溶液和脂质环境中的结果相反，Wakamatsu等人[Wakamatsu, K., Okada, A., Suzuki, M., Higashijima, T., Masui, Y., Sakakibara, S., & Miyazawa, T. (1986) Eur. J. Biochem. 154, 607 - 615]基于在D2O中的一维转移NOE研究提出了一种脂质环境构象，其中不包括β-转角。
