Conformationally constrained chemotactic peptide analogs of high biological activity

FEBS Letters

Freer, R.J.²  Balaram, P.³  Becker, E.L.¹  Showell, H.J.¹  Iqbal, M.³ 

[1] Department of Pathology University of Connecticut Health Center, Farmington, CT 06032, USA;Department of Pharmacology, Medical College of Virginia, Richmond, VA 23298, USA;Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India

关键词: Chemotactic peptide;    Neutrophil;    Chemotaxis;    Formylpeptide;   

DOI  :  10.1016/0014-5793(84)80163-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The stereochemically constrained chemotactic peptide analogs, formylmethionyl-α-aminoisobutyrylphenylalanine (formyl-Met-Aib-Phe-OH) and formylmethionylcycloleucinylphenylalanine (formyl-Met-Cyl-Phe-OH) are highly effective in inducing lysosomal enzyme release from rabbit neutrophils. NMR studies of the Aib² analog in (CD₃)₂SO favor a folded conformation in which the Phe NH group is inaccessible to solvent. Intramolecularly hydrogen-bonded conformations involving a Met-Aib-β-turn or a γ-turn centered at Aib² are considered. The results suggest that folded conformations may allow highly active interactions with the neutrophil formylpeptide receptor.

【 授权许可】

Unknown