SECONDARY STRUCTURE CHARACTERISTICS OF PROENKEPHALIN PEPTIDE-E, PEPTIDE-B, AND PEPTIDE-F

作     者：HIDDINGA, HJ KATZENSTEIN, GE MIDDAUGH, CR LEWIS, RV 

作者机构：UNIV WYOMING DEPT MOLEC BIOL BOX 3944 UNIV STN LARAMIE WY 82071 USA 

出 版 物：《NEUROCHEMICAL RESEARCH》 (神经化学研究)

年 卷 期：1990年第15卷第4期

页      面：393-399页

核心收录：

学科分类：0710[理学-生物学] 1001[医学-基础医学(可授医学、理学学位)] 07[理学] 071003[理学-生理学] 

基　　金：NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [K04NS000968, R01NS020185] Funding Source: NIH RePORTER NINDS NIH HHS [NS 00968, NS 20185] Funding Source: Medline 

主　　题：Opioid peptide enkephalin containing polypeptide conformation structure-function relationships 

摘      要：The conformations of three adrenal medullary enkephalin containing polypeptides (ECPs) were investigated to gain an understanding of their potential structure-activity relationships. Secondary structure characteristics of peptides E, B, and F were examined by circular dichroism (CD) under conditions designed to mimic both the soluble state and the anisotropic environment which exists at the biological effector site. Conformational differences between the three peptides were further examined by Fourier Treansform Infrared Spectroscopy (FTIR) and by empirical predictions for conformation and hydrophobic periodicity. Although all three peptides have a similar structure, existing in random configurations in aqueous solutions, they do exhibit unique individual potentials to assume secondary structure in less polar environments. These conformational differences may be important factors in determining their unique individual biological activities.