MEMBRANE BOUND TRYPTOPHAN DYNAMICS IN CECROPIN

天蚕素中的膜结合色氨酸动力学

• 批准号: 6281093
• 负责人: Paul H Axelsen
• 金额: $ 0.27万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-08-01 至 1999-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6281093
• 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 seeking to characterize 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是一种天然的线状抗菌肽 由昆虫幼虫产生；它具有强大的抗菌活性和 包括似乎是唯一抵抗细菌的宿主 这些生物体中的感染。作为生物物理阵列的一部分 对这些多肽作用机制的研究 他们的抗菌作用，我们正在寻求表征 单一色氨酸残基在游离态和游离态中的转动活性 利用时间分辨各向异性研究天蚕素A的膜结合形式 色氨酸侧链荧光的测量。