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US4488911A Expired / Lapsed US ⏱️ 0.0 years remaining

Non-antigenic collagen and articles of manufacture

Assignee: Angiotech Biomaterials Corp
•
Filing: 1983-09-15
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Granted: 1984-12-18
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Expires: 2003-09-15
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Abstract

Abstract Collagen, available from domestic animals, is freed of noncollagen proteins, glycosaminoglycans and lipids by enzymatic treatment with a proteolytic enzyme to yield a product which is soluble in dilute acidic aqueous solutions (collagen in solution--CIS). The naturally occurring collagen is modified by removal of certain terminal peptide chains, which are described as telopeptides. The modified collagen, so derived, is described as atelopeptide collagen. Native collagen is immunogenic, while atelopeptide collagen is nonimmunogenic or possessed of a negligibly low level of immunogenicity. The collagen in solution is then treated according to a specific regimen under conditions whereby the collagen slowly separates from solution while exposed to mild shear forces. This procedure results in the formation of a fibrous precipitate composed of regularly ordered fibers of collagen possessed of a rope-like structure. These resulting aggregates are referred to as native fibrous micropolymers (NFM). Once the regimen or procedure is completed, and the fiber mass has been formed, the fibrous micropolymers may be freed of salt, taken up in a different solution or modified. For example, cross-links may then be introduced to stabilize the fibers. The products find wide use as packing, membranes, fibers, bags, supports, integuments, and are especially suitable for biologic implantation or application.

Inventors

  • 👤 Edward E. Luck
  • 👤 John R. Daniels

Bibliographic Details

Application Number —
Jurisdiction US
Data Source google_patents
Last Synchronized 2026-10-23 17:12
CPC Classifications
A; A61; A61L; A61L15/00; A61L15/16; A61L15/22; A61L15/32; A61L15/325; A61L17/00; A61L17/06; A61L17/08; A61L26/00; A61L26/0009; A61L26/0028; A61L26/0033; A61L27/00; A61L27/14; A61L27/22; A61L27/24; C; C08; C08L; C08L89/00; C08L89/04; C08L89/06; D; D01; D01F; D01F4/00; A61F; A61F2310/00; A61F2310/00005; A61F2310/00365; Y; Y10; Y10S; Y10S530/00; Y10S530/827; Y10S530/84; Y10S530/842

Claims Analysis

Total Claims: 16
Claim 1
Independent Claim 56 words
A method of preparing fibers of atelopeptide collagen having physical properties resembling natural collagen fibers which comprises: inducing slow desolubilization of atelopeptide collagen from an aqueous solution of atelopeptide collagen while subjecting said solution to a directionally uniform mild shear force of about 30 to about 5000 dynes/cm 2 whereby fibers of atelopeptide collagen are formed.
Claim 2
Independent Claim 56 words
A method of preparing fibers of atelopeptide collagen having physical properties resembling natural collagen fibers which comprises: inducing slow desolubilization of atelopeptide collagen from an aqueous solution of atelopeptide collagen while subjecting said solution to a directionally uniform mild shear force of about 30 to about 5000 dynes/cm 2 whereby fibers of atelopeptide collagen are formed.
Claim 3
Dependent Claim 26 words
A method according to claim 1, wherein said inducing is achieved by having an initial acidic medium to which is slowly added an inorganic alkaline salt.
Claim 4
Dependent Claim 14 words
A method according to claim 2, wherein said inorganic alkaline salt is a phosphate.
Claim 5
Dependent Claim 27 words
A method according to claim 1, wherein said aqueous solution is contained in a dialysis bag which is slowly rotated in an aqueous inorganic alkaline salt medium.
Claim 6
Dependent Claim 25 words
A method according to claim 1, wherein said inducing is achieved by thermal gelation employing a salt solution at about physiological salt concentration and pH.
Claim 7
Dependent Claim 14 words
A method according to claim 1, including the step of cross-linking said isolated fibers.
Claim 8
Independent Claim 79 words
A method of preparing fibers of atelopeptide collagen fibrils having physical properties resembling natural collagen fibers which comprises: slowly adding to a dilute aqueous acidic solution of atelopeptide collagen an inorganic alkaline salt, whereby the ionic strength and pH of the solution are raised, while subjecting said solution to rotational shear forces of about 30 to 5000 dynes/cm 2 so that fibers of atelopeptide collagen fibrils come out of solution; and substantially freeing said fibers of said alkaline salt.
Claim 9
Independent Claim 79 words
A method of preparing fibers of atelopeptide collagen fibrils having physical properties resembling natural collagen fibers which comprises: slowly adding to a dilute aqueous acidic solution of atelopeptide collagen an inorganic alkaline salt, whereby the ionic strength and pH of the solution are raised, while subjecting said solution to rotational shear forces of about 30 to 5000 dynes/cm 2 so that fibers of atelopeptide collagen fibrils come out of solution; and substantially freeing said fibers of said alkaline salt.
Claim 10
Dependent Claim 13 words
A method according to claim 7, including the step of cross-linking said fibers.
Claim 11
Dependent Claim 19 words
A method according to claim 8, wherein said cross-linking agent is formaldehyde, glutaraldehyde, chromic sulfate, ultraviolet radiation or heat.
Claim 12
Dependent Claim 23 words
A method according to claim 7, wherein said shear force is produced by rotation of said solution at about 20 to 1000 rpm.
Claim 13
Dependent Claim 56 words
A method according to claim 10, wherein said aqueous acidic solution is an aqueous acetic acid solution at a concentration in the range of about 0.001 M to 0.1 M and said alkaline salt is disodium acid phosphate which is added to provide a final concentration in the range of about 0.01 M to 0.05 M.
Claim 14
Dependent Claim 29 words
The method of claim 1 wherein said fibers have a mean diameter of at least about 500 nm and appear as a rope-like structure in a scanning electron micrograph.
Claim 15
Dependent Claim 28 words
The method of claim 7 wherein said fibers have a mean diameter of at least 500 nm and appear as a rope-like structure in a scanning electron micrograph.
Claim 16
Dependent Claim 18 words
The method according to claim 1 wherein the shear force is about 75 to 2500 dynes/cm 2 .

References Cited (Backward Citations)

US2920000A Cited
US2919999A Cited
GB903975A Cited
US3131130A Cited
US3314861A Cited
US3503877A Cited
US3303038A Cited
US4089333A Cited
US3949073A Cited
US4140537A Cited
US4233360A Cited

USPTO Annuity & Maintenance Windows

Annuity Stage Window Opens Payment Deadline Surcharge Period Until Estimated Fee Status
3.5 Years (Year 4) 1987-12-18 1988-06-18 1988-12-18 $2000.00 Window Closed / Lapsed
7.5 Years (Year 8) 1991-12-18 1992-06-18 1992-12-18 $3760.00 Window Closed / Lapsed
11.5 Years (Year 12) 1995-12-18 1996-06-18 1996-12-18 $7700.00 Window Closed / Lapsed

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