MEMBRANE BOUND TRYPTOPHAN DYNAMICS IN CECROPIN

天蚕素中的膜结合色氨酸动力学

• 批准号: 6120152
• 负责人: Paul H Axelsen
• 金额: $ 0.11万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-08-01 至 2000-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6120152
• 关键词: biological products; biomedical resource; proteins

Cecropin A is a naturally occurring linear antimicrobial peptide produced by insect larvae; it has potent antimicrobial activity and comprises what appears to be the sole host defense against bacterial infection in these organisms. As part of an array of biophysical investigations into the mechanism by which these peptides accomplish their antimicrobial effect, we are characterizing the rotational activity of the single Trp residue in both free and membrane-bound forms of cecropin A using time-resolved anisotropy measurements of the Trp side chain fluorescence.

天蚕素A是一种天然存在的线性抗菌肽 由昆虫幼虫产生;它具有有效的抗菌活性， 似乎是宿主抵御细菌的唯一手段 感染这些生物。 作为一系列生物物理 研究这些肽实现 他们的抗菌效果，我们正在表征旋转 游离和膜结合中单个Trp残基的活性 使用时间分辨的各向异性测量的天蚕素A的形式 色氨酸侧链荧光。