H-Trp-(Pro)4-Tyr-OH | 62716-47-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: H-Trp-(Pro)4-Tyr-OH
• 英文别名: L-Tryptophyl-L-prolyl-L-prolyl-L-prolyl-L-prolyl-L-tyrosine；(2S)-2-[[(2S)-1-[(2S)-1-[(2S)-1-[(2S)-1-[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoic acid
• CAS: 62716-47-6
• 化学式: C₄₀H₄₉N₇O₈
• 分子量: 755.871
• InChiKey: KXLXBILACIGVAV-TZEHAJJTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  55
• 可旋转键数：
  11
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  210
• 氢给体数：
  5
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  H-Trp-(Pro)4-Tyr-OH 在 sodium azide 、 一氧化二氮 作用下， 以 水 为溶剂， 生成 H-Trp*-(Pro)4-Tyr-OH
  参考文献：
  名称：

  Pulse radiolysis studies of intramolecular electron transfer in model peptides and proteins. 5. Trp.bul. .fwdarw. Tyr.bul. radical transformation in H-Trp-(Pro)n-Tyr-OH series of peptides

  摘要：

  The kinetics of intramolecular long-range electron transfer (LRET) between neutral tryptophan radical and tyrosine in aqueous solution of H-Trp-(Pro)n-Tyr-OH, n = 4 and 5, peptides has been studied by pulse radiolysis over the temperature range 288-328 K. The rate constants, k1, and thermodynamic activation parameters of LRET thus obtained, together with those for shorter (n = 0-3) peptides of the same series, measured earlier, are analyzed in terms of Marcus nonadiabatic theory of LRET and distributions of donor-acceptor distances and angular orientations determined by the conformational energy calculations. To explain the observed exponential decrease of k1 with the number of n of Pro residues, simulation of the overall distance dependence of the rate according to models assuming involvement of LRET (i) through-bond (TB), (ii) through-space (TS), and also (iii) through both pathways simultaneously were performed by fitting the calculated mean rate constants, [k(TB)] and [k(TS)], to the experimental k1 data. The best agreement between the experimental and calculated rates was obtained for a modified version of the last model (iii), according to which competitive electron transfer through the TS pathway occurs only in the conformers exhibiting van der Waals contacts and favorable angular orientation for a large overlap of pi and sigma orbitals between the indole and phenol rings. The best-fit rate constants obtained indicate that in short-bridged peptides (n = 0-2) electron transfer takes predominantly the TS pathway, while in longer ones (n = 3-5) it occurs mainly by the TB pathway (beta(TB) = 0 28 +/- 0.05 angstrom-1 at 298 K). Descriptors of electronic (beta(el)TB almost-equal-to 0.2 angstrom-1) and nuclear (beta(n)TB almost-equal-to 0.1 angstrom-1) contributions to the overall distance dependence of the TB-LRET were roughly estimated from the distance dependence of activation parameters, derived from mte constants, k(l,cor), corrected for an expected thermal longitudinal expansion of the oligoproline bridge.

  DOI：

  10.1021/j100203a082