Modified mutant collagenase and its use in fat melting and in scar reduction
AssigneeYolare Pharmaceuticals, LLC
InventorsLan Huang, Yong Cang, Renato (Rene) Jose
Life of this patent
Estimating the term…
Loading patent…
AssigneeYolare Pharmaceuticals, LLC
InventorsLan Huang, Yong Cang, Renato (Rene) Jose
Estimating the term…
A Clostridium histolyticum collagenase ColH (Glu451Asp) melts adipose tissue when injected into selected regions of the body. This protein product melts fat pads effectively in fat rat experiments, with very little side effects. Very little hemorrhage was observed. We also invent a new version of ColH mutant by linking a peptide motif CKGGRAKDC-G (varying from 2 to 6 Gs) (SEQ ID NO: 2) in front of ColH (Glu451Asp) (called topical ColH-FM), which can target to white fat vasculature. By combining with novel transdermal technology (such as Hydroxysome technology), we develop a topical protein cream that can melt fat. This product can be used as cellulite cream and for chemical liposuction. This topical ColH-FM can also be injected into adipose tissue as a replacement for liposuction or as an adjunct method with liposuction. Since raise scar is formed by overgrowth of collagen, our topical ColH-FM cream is shown to have application in scar reduction.
A method for reducing the amount of adipose tissue at selected locations in the body comprising:
A method for reducing or removing lipomas comprising:
A method for reducing scars comprising:
Dependencies are inferred from the claim text.
Drawings are temporarily unavailable. Open the PDF at USPTO
From the US filing history. Foreign family members aren’t listed.
No references of this kind are recorded.
From bacteria: from Clostridium
Drugs for disorders of the metabolism
Drugs for disorders of the metabolism: anorexiants; Antiobesity agents
Drugs for dermatological disorders
About 2 years 3 months of term left · ends 23 Jan 2029 (estimated)
The invention relates to Modified mutant collagenase for fat melting application and for scar reduction application.
The instant application contains a Sequence Listing which has been submitted in ASCII format via EFS-Web and is hereby incorporated by reference in its entirety. Said ASCII copy, created on Jan. 30, 2012, is named 8254002.txt and is 26,614 bytes in size.
1) Fat Reduction
FIGs. 1A to 1H describe Mutant ColH (E451D) and modified mutant ColH (E451D) (ColH-FM) protein and DNA sequences. In particular, FIG. 1A shows SEQ ID NO: 10, FIG. 1B shows SEQ ID NOS: 10 and 11, FIGS. 1C-1E show SEQ ID NO: 12, and FIGS. 1F-1H show SEQ ID NO: 13.
FIG. 2 describes proposed active site of ColH. The zinc-coordinating bonds and hydrogen bonds are indicated by thick arrows and dotted lines, respectively. Thin arrows represent the first steps of the mechanism of action (Derived from J. Bacteriology, May 1999, p. 2816-2822).
FIG. 3 is the electrophoresis photo with 7.5% PAGE gel of purified ColH (E451D) and stability results of wild type ColH and mutant ColH (E451D). Native ColH (10 ug) was incubated with Trypsin (1 ug) at lane 1, incubated with Trypsin (2 ug) at lane 2 both for 1 hour at 4 C. ColH (E451D, 10 ug) was incubated with Trypsin (0.5 ug) at lane 3, incubated with Trypsin (1 ug) at lane 4, incubated with Trypsin (2 ug) at lane 5 all for 1 hour at 4 C. After 1 hour of incubation, the digestion reaction was stopped with 0.5 ul of 0.1 M PMSF. Each incubation was examined by running 7.5% SDS-PAGE.
1. Cloning of ColH (GST-ColH, Using pGEX5T-3 Plasmid)
1) DNA of ColH from Dr. Matsushita of Kagawa Medical School, Japan (2 ug, pCHC11)
2) PCR using primers below to get a 2.95 kb DNA fragment (A87) using ColH DNA as template (from Dr. Matsushita).