Hengguang G Li

US Patent:

7604804, Oct 20, 2009

Filed:

Feb 9, 2005

Appl. No.:

11/054398

Inventors:

Lai-Xi Wang - Ellicott City MD, US
Hengguang Li - Lutherville MD, US

Assignee:

University of Maryland Biotechnology Institute - Baltimore MD

International Classification:

A61K 39/385
A61K 39/12
A61K 39/21

US Classification:

4241841, 4241931, 42419611, 4242041, 4242071, 4242081

Abstract:

The present invention relates to multivalent HIV inhibitors that bind to multiple sites on a trimeric gp120 complex thereby blocking the CD4 binding site on the trimeric gp120 complex and inhibiting the attachment and entry of HIV through gp120-CD4 interactions.

US Patent:

8198434, Jun 12, 2012

Filed:

May 5, 2009

Appl. No.:

12/435462

Inventors:

Yerramilli V. S. N. Murthy - Apex NC, US
Edward Obare - Portland ME, US
Hengguang Li - Morrisville NC, US

Assignee:

IDEXX Laboratories, Inc. - Westbrook ME

International Classification:

C07D 501/54

US Classification:

540224

Abstract:

The invention is directed to an improved process for preparing cefsulodin sodium. The process involves: (i) dissolving cefsulodin in a solvent comprising an organic solvent to provide a solution of cefsulodin, (ii) adding about 1 equivalent of a sodium salt of a base to the solution of cefsulodin to provide a solution of cefsulodin sodium, and (iii) separating the cefsulodin sodium from the solution of cefsulodin sodium.

US Patent:

20050159341, Jul 21, 2005

Filed:

Jun 20, 2003

Appl. No.:

10/518108

Inventors:

Lai-Xi Wang - Ellicott City MD, US
Jianghong Ni - Baltimore MD, US
Hengguang Li - Baltimore MD, US
Sudham Singh - Chapel Hill NC, US

International Classification:

A61K038/16
A61K031/724
C07K009/00
C07D487/22
C07D043/14

US Classification:

514008000, 514058000, 530322000, 536046000, 536103000, 540145000, 548517000

Abstract:

Disclosed are scaffolded maleimide clusters, methods of making said clusters and use of said clusters as templates for multivalent peptide assembly. Multiple maleimide functionalities were introduced onto a scaffold molecule by the reaction of a core-centered polyamines with methoxycarbonylmaleimide or with activated esters of maleimide-containing compounds. The scaffolded maleimides allow rapid, highly chemoselective, and high-yield ligation with thiolcontaining peptides under virtually neutral conditions at room temperature. The disclosed mild and highly efficient ligation method is extremely valuable for synthesizing large and complex multivalent peptides that may not be easily obtained by conventional ligation methods. These novel scaffolded maleimide clusters allow a highly chemoselective ligation with a thiolcontaining peptide under virtually neutral conditions, providing a new and efficient approach for multivalent peptide assembly. The disclosed mild and highly efficient ligation method is extremely valuable for synthesizing large and complex multivalent peptides that may not be easily obtained by conventional ligation methods. A series of multivalent peptides containing the sequence of the 36-mer HIV-1 inhibitor DP178 (T20), the T-helper epitope from tetanus toxoid (830-844), and the minimum epitope sequence of the potent HIV-neutralizing antibody 2F5 were synthesized. Carbohydrates and cholic acid were chosen as the scaffold because of their rigidity and mufti-functionality. Thus, the topology of the multivalent peptides can be controlled by the defined spatial orientation of the maleimide functionalities on the rigid scaffold core. The resulting multivalent gp41 peptides incorporating strands of DP178 on the monosaccharide and the cholic acid templates were found to be able to form three or four a-helix bundles. Moreover, the multivalent peptides containing strands of the long gp41 peptide DP178 were highly immunogenic and were able to raise high titers of peptide-specific antibodies in the absence of any additional adjuvant. Therefore, these and related multivalent peptides constructed on the maleimide clusters may be used as novel immunogens, potential inhibitors, protein mimics, artificial proteins, and powerful antigens for a broad range of biomedical applications.