Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
Biochem Biophys Res Commun. 2012 Jul 27;424(2):290-4. doi: 10.1016/j.bbrc.2012.06.109. Epub 2012 Jun 27.
Vascular Endothelial Growth Factor mimetic peptides have interesting applications in therapeutic angiogenesis. Recently, we described the proangiogenic properties of a 15 mer peptide designed on the N-terminal helix 17-25 of VEGF. The peptide was stabilized introducing well known peptide chemical tools among which N- and C-terminal capping sequence. Here, we show that the C-terminal sequence does not affect the structural and biological properties of the full-length peptide. In fact, a C-terminal truncated analog peptide resulted in a well folded and stable helix retaining the ability to bind to VEGF receptors. This study will allow to develop smaller peptidomimetic analogs able to modulate the VEGF-dependent angiogenesis.
血管内皮生长因子模拟肽在治疗性血管生成中有重要的应用。最近，我们描述了一种 15 肽的促血管生成特性，该肽是基于 VEGF 的 N 端螺旋 17-25 设计的。通过引入众所周知的肽化学工具，如 N 和 C 端封端序列，使该肽稳定化。在此，我们证明 C 端序列不影响全长肽的结构和生物学特性。事实上，C 端截断类似物肽形成了一个折叠良好且稳定的螺旋结构，保留了与 VEGF 受体结合的能力。这项研究将有助于开发更小的肽模拟物类似物，以调节 VEGF 依赖性血管生成。
