Position one analogs of the Saccharomyces cerevisiae tridecapeptide pheromone.
Position one analogs of the Saccharomyces cerevisiae tridecapeptide pheromone.
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酿酒酵母十三肽信息素的位置一类似物。
DOI：
10.1111/j.1399-3011.1997.tb01190.x
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Naider,F
中科院分区：
文献类型：
--
作者：
Zhang,YL;Lu,HF;Becker,JM;Naider,F
合成了多种残基取代色氨酸的酿酒酵母α交配因子类似物[WHWLQLKPGQPMY]，并对其生物活性和受体亲和力进行了测定。在生长抑制实验中，含有Gly或Leu的类似物或在肽的第1位含有许多不同的芳香族残基的生物活性略大于或等于亲本信息素的生物活性，而Glu和Lys类似物的生物活性显著低于亲本信息素。1位芳香族取代的类似物的受体亲和力比母肽低3-6倍，而N-末端有亲水性残基的类似物与位置1的谷氨酸的受体亲和力显著降低120倍。N-α-乙酰化对生物活性影响不大，但使受体亲和力降低20-40倍。羧基末端的酰胺化导致活性降低10倍，受体亲和力降低160倍。这些结果表明，α-因子受体有一个大的疏水结合口袋，可能含有一个带负电荷的侧链，该侧链与α-因子的N端相互作用。一些类似物的活性和结合之间缺乏相关性，这表明在信号转导途径的第一步，α-因子N端附近的小残基可能非常有效地触发受体异构化到其激活状态。©孟克斯加德1997年。
Analogs of theSaccharomyces cerevisiaeα‐mating factor [WHWLQLKPGQPMY]., in which a variety of residues replaced Trp were synthesized and assayed for biological activity and receptor affinity. Analogs containing Gly or Leu or many different aromatic residues in position 1 of the peptide exhibited bioactivity in a growth arrest assay slightly greater than, or equal to, that of the parent pheromone, whereas the Glu and Lys analogs exhibited significantly lower bioactivity. Analogs with an aromatic replacement at position 1 had 3‐ to 6‐fold lower receptor affinity than the parent peptide, whereas analogs with a hydrophilic residue at the N‐terminus exhibited large reductions in receptor affinity with the peptide with Glu in position I showing a 120‐fold reduction.Nα‐Acetylation had little effect on bioactivity but lowered receptor affinity by 20‐ to 40‐fold. Amidation of the carboxyl terminus resulted in a 10‐fold decrease in activity and a 160‐fold decrease in receptor affinity. These results indicate that the α‐factor receptor has a large hydrophobic binding pocket, possibly containing a negatively charged side‐chain, which interacts with the N‐terminus of a‐factor. The lack of correlation between activity and binding of several analogs suggests that small residues near the N‐terminus of a‐factor may be very efficient in triggering isomerization of the receptor to its activated state in the first step of the signal transduction pathway. © Munksgaard 1997.