Synthesis and receptor binding of opioid peptide analogues containing β3‐homo‐amino acids
Synthesis and receptor binding of opioid peptide analogues containing β3‐homo‐amino acids
复制标题
含有β3-同型氨基酸的阿片肽类似物的合成和受体结合
作者：
D. Wilczyńska;P. Kosson;Maria Kwasiborska;A. Ejchart;A. Olma
含有杂合肽和β-肽的β-氨基酸显示出作为肽模拟物的巨大潜力。在本文中，我们描述了β肽的合成及其对μ-和δ-阿片受体的亲和力，β肽是亮脑啡肽类似物，deltorphin I，dermorphin和α，β-hybrides，deltorphin I的类似物。用β3-高氨基酸残基取代α-氨基酸残基通常会导致对阿片受体的亲和力降低。然而，在deltorphin I的2位掺入β 3 h-D-Ala或在3位掺入β 3 hPhe导致δ-阿片受体的有效和选择性配体。β-deltorphin I类似物的NMR研究表明，肽骨架中心部分的构象运动受到部分限制，并且可以预期一些构象偏好。版权所有© 2009年欧洲肽协会和约翰威利父子有限公司。
β‐Amino acids containing hybrid peptides and β‐peptides show great potential as peptidomimetics. In this paper we describe the synthesis and affinity toward the µ‐ and δ‐opioid receptors of β‐peptides, analogues of Leu‐enkephalin, deltorphin I, dermorphin and α,β‐hybrides, analogues of deltorphin I. Substitution of α‐amino acid residues with β3‐homo‐amino acid residues, in general resulted in decrease of affinity to opioid receptors. However, the incorporation β3h‐D‐Ala in position 2 or β3hPhe in position 3 of deltorphin I resulted in potent and selective ligand for δ‐opioid receptor. The NMR studies of β‐deltorphin I analogue suggest that conformational motions in the central part of the peptide backbone are partially restricted and some conformational preferences can be expected. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.
通过尿素桥限制的德尔托芬类似物：结构和阿片类药物活性。
DOI：
10.1002/psc.1010
发表时间：
2008
期刊：
Journal of peptide science : an official publication of the European Peptide Society
影响因子：
--
作者：
Zieleniak,Agnieszka;Rodziewicz-Motowidło,Sylwia;Rusak,Lukasz;Chung,NgaN;Czaplewski,Cezary;Witkowska,Ewa;Schiller,PeterW;Ciarkowski,Jerzy;Izdebski,Jan
通讯作者：
Izdebski,Jan
影响因子：
3.5
作者：
Koda, Yasuko;Del Borgo, Mark;Blanchfield, Joanne T.
通讯作者：
Blanchfield, Joanne T.