生物活性肽：[酪氨酸4]环林诺肽A的构象研究

Bioactive peptides: conformational studies of [Tyr4] cyclolinopeptide A.

作者信息

Saviano M, Rossi F, Filizola M, Isernia C, Di Blasio B, Benedetti E, Pedone C, Siemion I Z, Pedyczak A

机构信息

CNR, Università di Napoli Federico II, Dipartimento di Chimica, Italy.

出版信息

Biopolymers. 1995 Oct;36(4):453-60. doi: 10.1002/bip.360360408.

DOI:10.1002/bip.360360408

PMID:7578940

Abstract

The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [alpha = 9.849 (5) A, b = 20.752 (4) A, c = 16.728 (5) A, beta = 98.83 (3) degrees, space group P21, Z = 2], shows the presence of five intramolecular N-H...O = C hydrogen bonds, with formation of one C17 ring structure, one alpha-turn (C13), one inverse gamma-turn (C7), and two beta-turns (C10, one of type III and one of type I). The Pro1-Pro2 peptide unit is cis (omega = 5 degrees), all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 A.

摘要

通过X射线衍射研究对[酪氨酸4]环脂肽A进行了固态构象分析。从二氧六环 - 水混合物中生长出的单斜晶系形式的晶体结构[α = 9.849(5)Å，b = 20.752(4)Å，c = 16.728(5)Å，β = 98.83(3)°，空间群P21，Z = 2]显示存在五个分子内N - H...O = C氢键，形成一个C17环结构、一个α - 转角(C13)、一个反向γ - 转角(C7)和两个β - 转角(C10，一个III型和一个I型)。Pro1 - Pro2肽单元是顺式(ω = 5°)，其他所有都是反式。该结构与环脂肽A的结构几乎完全重叠。主链原子的均方根偏差平均为0.33Å。