1. Crosslink-free collagen from Cichla ocellaris: Structural characterization by FT-IR spectroscopy and densitometric evaluation
- Author
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Ana Lúcia Figueiredo Porto, Caio Rodrigo Dias de Assis, Helane Maria Silva Costa, Ranilson de Souza Bezerra, Nathalia Albuquerque Roberto, Juliana Ferreira dos Santos, Flávia Thuane Duarte do Monte, Robson Coelho de Araújo Neri, and Vagne Melo Oliveira
- Subjects
chemistry.chemical_classification ,biology ,Absorption spectroscopy ,010405 organic chemistry ,Hydrogen bond ,Cichla ocellaris ,Organic Chemistry ,Salt (chemistry) ,010402 general chemistry ,biology.organism_classification ,01 natural sciences ,0104 chemical sciences ,Analytical Chemistry ,Inorganic Chemistry ,chemistry.chemical_compound ,Electrophoresis ,Crystallography ,chemistry ,Amide ,Fourier transform infrared spectroscopy ,Densitometry ,Spectroscopy - Abstract
Crosslink-free collagen of skin from peacock bass Cichla ocellaris was successfully isolated and had its structural characteristics analyzed mainly by the combination of two techniques: optical densitometry and FT-IR. The optical densitometry coupled to the electrophoretic profile showed two typical α chains (α1 and α2), lower content of dimmers and trimmers (β and ɣ chain, respectively) than other extraction methods and without formation of high molecular weight crosslinks (HMC and VMC). UV–visible absorption spectrum was 211 nm. FT-IR spectra analysis of the amide A, amide B, amide Ι, amide ΙI and amide ΙΙI bands were 3276, 2930, 1637, 1547 and 1240 cm−1, respectively, and showed maintenance of the triple helical chain stabilized by hydrogen bonds characterizing it as collagen. Moreover, PSC was soluble in the range from 0 to 3% of salt concentrations, as well as in alkaline media (pH 8). Our results indicate that the two main techniques used were able to identify and characterize the type 1 crosslinks-free collagen from C. ocellaris, which may be suitable for applications that requires higher purification degree.
- Published
- 2019
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