Bianca Rose Sculimbrene

20030100090, May 29, 2003

Jul 1, 2002

10/187208

Scott Miller - Natick MA, US
Bianca Sculimbrene - Newton MA, US
Adam Morgan - N. Scituate RI, US

The Trustees of Boston College

C12N009/16

435/196000

The present invention provides peptide-based phosphorylation catalysts (PBPC's) for the asymmetric monophosphorylation of cyclitols, particularly myo-inositols. The PBPC's of the invention effect a regio and enantioselective phosphorylation of a myo-inositol in a manner analogous to enzymatic kinases, thereby functioning as effective “kinase mimics.” Although orders of magnitude less complex in terms of structure than macromolecular proteins, the PBPC's of the invention control product formation with high enantioselectivity ( 98% ee). The synthetic (+)-myo-inositol-1-phosphate is optically and spectroscopically equivalent to naturally occuring compound. The ability of the low molecular weight PBPC's of the present invention to mimic stereoselective enzymes represents a powerful approach toward catalytic asymmetric synthesis of biologically important molecules, and for mechanistic modeling of biochemical transformations to enable their use in drug applications.

20050267291, Dec 1, 2005

Jul 11, 2005

11/178661

Scott Miller - Needham MA, US
Bianca Sculimbrene - Newton MA, US
Adam Morgan - North Scituate RI, US

C07K005/06
C07K007/06
C07K005/04

530329000, 530330000, 530331000, 548335500

The present invention provides peptide-based phosphorylation catalysts (PBPC's) for the asymmetric monophosphorylation of cyclitols, particularly myo-inositols. The PBPC's of the invention effect a regio and enantioselective phosphorylation of a myo-inositol in a manner analogous to enzymatic kinases, thereby functioning as effective “kinase mimics.” Although orders of magnitude less complex in terms of structure than macromolecular proteins, the PBPC's of the invention control product formation with high enantioselectivity (>98% ee). The synthetic (+)-myo-inositol-1-phosphate is optically and spectroscopically equivalent to naturally occurring compound. The ability of the low molecular weight PBPC's of the present invention to mimic stereoselective enzymes represents a powerful approach toward catalytic asymmetric synthesis of biologically important molecules, and for mechanistic modeling of biochemical transformations to enable their use in drug applications.