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首页> 外文期刊>Biochemistry >Single Disulfide and Linear Analogues Corresponding to the Carboxy-Terminal Segment to ovine beta-Defensin-2: Effects of Introducing the beta-Hairpin Nucleating Sequence D-Pro-Gly on Antibacterial Activity and Biophysical Propeties
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Single Disulfide and Linear Analogues Corresponding to the Carboxy-Terminal Segment to ovine beta-Defensin-2: Effects of Introducing the beta-Hairpin Nucleating Sequence D-Pro-Gly on Antibacterial Activity and Biophysical Propeties

机译：对应于羧基末端段对卵泡β-防御素-2的单二硫和线性类似物：在抗菌活性和生物物理化合物上引入β-发夹核序列D-Pro-Ply的效果

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摘要

Mammalian defensins (alpha as well as beta forms) have a beta-hairpin structural motif spanning approximately 20 residues at the carboxy-terminal end. We have investigated the antibacterial activity and biophysical properties of synthetic peptides corresponding to the carboxy-terminal segment of bovine beta-defensin-2 (BNBD-2): VRNHVTC_1RINRGFC_2VPIRC_3PGRTRQIGTC_4FGPRIKC_5C_6RSW (positions of disulfide bonds are C_1-C_5, C_2-C_4, and C_3-C_6). The parent sequence chosen was RCPGRTRQIGTIFGPRIKCRSW(PI), which spans the carboxy-terminal region of BNBD-2. Since the dipeptide sequence D-Pro-Gly favors nucleation of beta-hairpin structures even in acyclic peptides, analogues of P1 with one D-Pro-Gly at the central portion and two D-Pro-Gly segments near the N- and C- terminal ends were generated. An analogue in which GP (residues 14 and 15) in P1 was switched to PG was also synthesized. It was observed that the cyclic form as well as their linear forms exhibited antibacterial activity. Circular dichroism and theoretical studies indicated that while the beta-hairpin conformation is populated, there is conformational plasticity in the cyclic and linear peptides. The mode of bacterial killing was by membrane permeabilization. The entire mammalian defensin sequence does not appear to be essential for manifestation of antibacterial activity. Hence, short peptides corresponding to the C-terminal segments of mammalian defenses could have potential as therapeutic agents.
机译：哺乳动物Defensins（α以及β形成）具有诸如羧基末端约20个残基的β-发夹结构基质。我们研究了对应于牛β - 防御液-2（BNBD-2）的羧基末端区段的合成肽的抗菌活性和生物物理性质（BNBD-2）：VRNHVTC_1RINRGFC_2VPIRC_3PGRTRQIGTC_4FGPRIKC_5C_6RSW（二硫键的位置是C_1-C_5，C_2-C_4和C_3- C_6）。选择的父序列是RCPGRTRQIGTIFGPRIKCRSC（PI），其跨越BNBD-2的羧基末端区域。由于二肽序列D-Pro-Gly甚至在非循环肽中的β-发夹结构的成核，P1的类似P1的类似物在中央部分和靠近N-和C-附近的两个D-Pro-Gly段。产生终端结束。还合成了将P1中的GP（残基14和15）切换到PG的类似物。观察到循环形式以及它们的线性形式表现出抗菌活性。圆形二中间和理论研究表明，虽然填充了β-发夹构象，但在环状和线性肽中存在构象的可塑性。细菌杀伤模式是通过膜透析化。整个哺乳动物防御素序列似乎对抗菌活性的表现至关重要。因此，对应于哺乳动物防御的C末端区段的短肽可以具有潜力作为治疗剂。

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  • 来源
    《Biochemistry》 |2003年第31期|共9页
  • 作者

    Viswanatha Krishnakumari; Ambure Sharadadevi; Shashi Singh; Ramakrishnan Nagaraj;

  • 作者单位

    Centre for Cellular and Molecular Biology Uppal Road Hyderabad 500 007 India;

    Centre for Cellular and Molecular Biology Uppal Road Hyderabad 500 007 India;

    Centre for Cellular and Molecular Biology Uppal Road Hyderabad 500 007 India;

    Centre for Cellular and Molecular Biology Uppal Road Hyderabad 500 007 India;

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  • 正文语种 eng
  • 中图分类 生物化学;
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