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将 VEGF 模拟螺旋肽中的 N-封端区域全部由 L-氨基酸替换为 D-氨基酸。

Switching the N-Capping Region from all-L to all-D Amino Acids in a VEGF Mimetic Helical Peptide.

机构信息

Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via Pietro Castellino 111, 80131 Napoli, Italy.

CESTEV, Università di Napoli "Federico II", Via de Amicis 95, 80134, Napoli, Italy.

出版信息

Molecules. 2022 Oct 17;27(20):6982. doi: 10.3390/molecules27206982.

Abstract

The N-capping region of an α-helix is a short N-terminal amino acid stretch that contributes to nucleate and stabilize the helical structure. In the VEGF mimetic helical peptide QK, the N-capping region was previously demonstrated to be a key factor of QK helical folding. In this paper, we explored the effect of the chiral inversion of the N-capping sequence on QK folding, performing conformational analysis in solution by circular dichroism and NMR spectroscopy. The effect of such a modification on QK stability in serum and the proliferative effect were also evaluated.

摘要

α-螺旋的 N-端帽区是一段较短的 N 端氨基酸延伸,有助于成核并稳定螺旋结构。在 VEGF 模拟螺旋肽 QK 中,N-端帽区先前被证明是 QK 螺旋折叠的关键因素。在本文中,我们通过圆二色性和 NMR 光谱研究了 N-端帽序列手性反转对 QK 折叠的影响,在溶液中进行构象分析。还评估了这种修饰对 QK 在血清中的稳定性和增殖作用的影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a1cb/9607104/8573dca3687f/molecules-27-06982-g001.jpg

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