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US5332475A Expired / Lapsed US ⏱️ 0.0 years remaining

Cross-linking collagenous product

Assignee: University of North Carolina at Chapel Hill
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Filing: 1992-03-12
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Granted: 1994-07-26
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Expires: 2012-03-12
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Abstract

Abstract The present invention relates to a process for cross-linking a proteinaceous material. The process comprises: i) soaking the material to be cross-linked in an agueous solution of high osmolality; ii) incubating the material in an agueous buffer including an amount of a photooxidative catalyst sufficient to catalyze photooxidation of the material; and iii) irradiating the material and the catalyst of step (i) with light that includes a range of wavelengths selectively absorbed by the catalyst. Irradiation is effected under conditions such that cross-linking of the material occurs. In a further embodiment, the present invention relates to a cross-linked product produced by the above-described method.

Inventors

  • 👤 Gerald L. Mechanic

Bibliographic Details

Application Number —
Jurisdiction US
Data Source google_patents
Last Synchronized 2026-10-23 16:58
CPC Classifications
A; A61; A61L; A61L27/00; A61L27/36; A61L27/3683; A61L27/3687; C; C08; C08H; C08H1/00; C08H1/06

Claims Analysis

Total Claims: 11
Claim 1
Independent Claim 139 words
The stuble cross-linked collagenous product produced by the process comprising the steps of: soaking a collagenous tissue sample in an aqueous medium; immersing the soaked sample in an aqueous buffer including a photooxidative catalyst capable of donating electrons to the amino acids comprising the collagen fibrils of the collagenous tissue sample when excited by incident light to form either inter- or intramolecular or inter- and intra-molecular cross-links; and irradiating the soaked sample in an aqueous buffer including the catalyst with light while maintaining the oxygen concentration of the aqueous buffer so as to sensitize the catalyst into an excited state which is reduced by oxidative cross-linking of the amino acids comprising the collagenous tissue sample, the pH being maintained at between about 6.8 and about 8.6 and the temperature being maintained at between about -2° and about 50° C.
Claim 2
Dependent Claim 139 words
The stuble cross-linked collagenous product produced by the process comprising the steps of: soaking a collagenous tissue sample in an aqueous medium; immersing the soaked sample in an aqueous buffer including a photooxidative catalyst capable of donating electrons to the amino acids comprising the collagen fibrils of the collagenous tissue sample when excited by incident light to form either inter- or intramolecular or inter- and intra-molecular cross-links; and irradiating the soaked sample in an aqueous buffer including the catalyst with light while maintaining the oxygen concentration of the aqueous buffer so as to sensitize the catalyst into an excited state which is reduced by oxidative cross-linking of the amino acids comprising the collagenous tissue sample, the pH being maintained at between about 6.8 and about 8.6 and the temperature being maintained at between about -2° and about 50° C.
Claim 3
Dependent Claim 91 words
A stable cross-linked product produced by the method comprising the steps of: soaking collagen fibrils in a buffered medium having a neutral to alkaline pH which does not denature the collagen fibrils for a period of time sufficient to equilibrate the concentration of collagen with the concentration of a photooxidative catalyst solubilized in the medium, and thereafter oxidizing the collagen fibrils to form cross-linkages therebetween by inducing the transfer of electrons from the photooxidative catalyst to the collagen fibrils in the present of oxygen by exposing the collagen fibrils to light.
Claim 4
Dependent Claim 91 words
A stable cross-linked product produced by the method comprising the steps of: soaking collagen fibrils in a buffered medium having a neutral to alkaline pH which does not denature the collagen fibrils for a period of time sufficient to equilibrate the concentration of collagen with the concentration of a photooxidative catalyst solubilized in the medium, and thereafter oxidizing the collagen fibrils to form cross-linkages therebetween by inducing the transfer of electrons from the photooxidative catalyst to the collagen fibrils in the present of oxygen by exposing the collagen fibrils to light.
Claim 5
Dependent Claim 16 words
The product of claim 2 wherein the medium is buffered to a pH of about 7.4.
Claim 6
Dependent Claim 15 words
The product of claim 2 wherein the concentration of catalyst ranges from about 0.0001%-0.25% (wt/vol.).
Claim 7
Dependent Claim 22 words
The produce to claim 2 wherein the collagen fibrils are photooxidized at a temperature of from about -2° C. to +40° C.
Claim 8
Dependent Claim 20 words
The product of claim 2 wherein the collagen fibrils are exposed to light for about 2.5 to about 160 hours.
Claim 9
Dependent Claim 27 words
The product of claim 2 wherein the temperature of the medium is maintained at a selected temperature during the time the collagen fibrils are exposed to light.
Claim 10
Dependent Claim 15 words
The product of claim 1 wherein the concentration of catalyst ranges from about 0.001%-0.25% (wt/vol.).
Claim 11
Dependent Claim 20 words
The product of claim 1 wherein the collagenous sample is exposed to light for about 2.5 to about 160 hours.

References Cited (Backward Citations)

US3152976A Cited
US4835258A Cited
US5024742A Cited

USPTO Annuity & Maintenance Windows

Annuity Stage Window Opens Payment Deadline Surcharge Period Until Estimated Fee Status
3.5 Years (Year 4) 1997-07-25 1998-01-24 1998-07-26 $2000.00 Window Closed / Lapsed
7.5 Years (Year 8) 2001-07-25 2002-01-24 2002-07-26 $3760.00 Window Closed / Lapsed
11.5 Years (Year 12) 2005-07-25 2006-01-24 2006-07-26 $7700.00 Window Closed / Lapsed

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