Can grafting of an octapeptide improve the structure of a de novo protein?

FEBS Letters

Aphasizheva, Inna Yu¹  Kirpichnikov, Mikhail P¹  Dolgikh, Dmitry A¹  Ptitsyn, Oleg B²  Abdullaev, Ziedulla K¹  Uversky, Vladimir N² 

[1] Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117871 Moscow, Russia;Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia

关键词: De novo protein;    Molten globule;    Protein expression;    Protein design;    Interferon;   

DOI  :  10.1016/S0014-5793(98)00201-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Structural properties and conformational stability of de novo proteins – albebetin and albeferon (albebetin with a grafted interferon fragment) – were studied by means of CD spectroscopy, gel filtration and urea-induced unfolding. The results allow us to conclude that albebetin possesses the properties of the molten globule state. Grafting of the octapeptide to the N-terminus of this de novo protein affects its structure. We show here that albeferon maintains a secondary structure content of albebetin; it becomes more compact and much more stable toward urea-induced unfolding as compared to albebetin and even possesses some weak tertiary structure (at least around Tyr⁷). This means that the structure of the artificial protein albebetin can be improved by a simple procedure of octapeptide grafting to its N-terminus.

【 授权许可】

Unknown