Ultrathin collagen and gelatin fibers
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2023
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LATIN-AMERICAN CONGRESS OF ARTIFICIAL ORGANS AND BIOMATERIALS, 12th
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Introduction and objective: The main constituent of extracellular matrix (ECM) of various tissues is collagen,
a biodegradable and biocompatible protein with excellent regenerative properties. A promising way to
produce scaffolds, artificial ECM, involves the production of nanometric or submicrometric fibers, dimension
of the natural fibers found in the ECM of many tissues. Solution blow spinning (SB-Spinning) allows the
production of fibers with high feed rates and in situ deposition. Here we produce ultrathin collagen and
gelatin (polymer obtained from collagen denaturation) fibers by SB-Spinning using solvents that preserve the
integrity of the polymers and evaluate the morphology and properties of these fibers [1,2].
Methodology: Collagen (10 wt%) and gelatin (10 and 15 wt%) solutions were prepared in 90 wt% acetic acid
under stirring overnight at room temperature. A glass syringe was used to spin 25 cm (for gelatin) or 20 cm
(for collagen) away from the collector using 30 psi (gelatin) or 10 psi (collagen) of pressure at 3.6 to 10.8
mL/h for gelatin and at 3 to 6 mL/h for collagen. The fibers were characterized by scanning electron
microscopy, differential scanning calorimetry and polyacrylamide gel electrophoresis.
Results and discussion: Gelatin and collagen submicrometric fibers were produced from 90% acetic acid
solutions, a benign solvent that allows the solubilization of high amounts of these polymers and present low
toxicity with low cost, what reveals it as a promising benign solvent for this application. Gelatin fibers
presented average diameters between 740 ± 299 nm and 909 ± 326 nm for 15% solutions and between 175
± 64 nm and 196 ± 113 nm for 10% solutions, indicating the direct effect of polymer concentration on the
diameter of fibers. Collagen fibers presented average diameters between 542 ± 185 nm and 543 ± 242 nm,
being thicker than the gelatin fibers obtained with the same polymer concentration, an indicative of the
preservation of the natural structure of these protein, the triple helix secondary structure. The preservation
of collagen triple helix after the spinning process was confirmed by differential scanning calorimetry and gel
electrophoresis results.
Conclusions: Aqueous acetic acid was considered a good solvent for the solubilization of these collagenous
proteins, being adequate to the production of biomaterials due to its low toxicity and ability to preserve the
natural structure of collagen. It was also possible to understand the effect of some production parameters
on the diameter of these fibers, an important step in the development of new biomimetic biomaterials
produced by solution blow spinning.
Como referenciar
RODRIGUES, MURILO A.V.; MARTINS, VIRGINIA da C.A.; LUGAO, ADEMAR B.; MATTOSO, LUIZ H.C.; PLEPIS, ANA M. de G. Ultrathin collagen and gelatin fibers: benign solvents to produce potential biomimetic biomaterials by solution blow spinning. In: LATIN-AMERICAN CONGRESS OF ARTIFICIAL ORGANS AND BIOMATERIALS, 12th, December 12-15, 2023, Mar del Plata, Argentina. Abstract... p. 45-45. Disponível em: https://repositorio.ipen.br/handle/123456789/47953. Acesso em: 30 Dec 2025.
Esta referência é gerada automaticamente de acordo com as normas do estilo IPEN/SP (ABNT NBR 6023) e recomenda-se uma verificação final e ajustes caso necessário.