Preparation and Structural Analysis of Actinidain-processed Atelocollagen of Yellowfin Tuna (<i>Thunnus albacares</i>)

Morimoto, Katsura; Kunii, Saori; Hamano, Kaori; Tonomura, Ben’ichiro

doi:10.1271/bbb.68.861

Cited by 15 publications

(15 citation statements)

References 31 publications

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“…AHCol can be considered as an essentially monomeric collagen in which 58% of molecules are composed of two ␣1 chains and 32% of ␣2 chains, with few cross-linkages between ␣ chains. These results are consistent with our previous data on tuna AHCol (30,31).…”

Section: Discussionsupporting

confidence: 94%

“…CD Spectrum of ASCol, PHCol, and AHCol-The triple-helical structure of each of ASCol, PHCol, and AHCol (prepared as described above) was confirmed by CD spectra as reported (30,31). The far-UV CD spectrum of the collagen preparations was measured by scanning through the range of 200 -250 nm with a CD spectropolarimeter J-820 (JASCO, Tokyo, Japan).…”

Section: Methodsmentioning

confidence: 92%

“…In this study, we compared the structural features of two types of protease-hydrolyzed collagen molecules, PHCol and AHCol, obtained from limited hydrolysis by pepsin and actinidain, respectively, from chicken skinderived ASCol. These collagen preparations were chosen because PHCol and AHCol derived similarly from tuna skin show interesting structural differences (30,31). Full sequence information of tuna skin collagen is not available.…”

Section: Discussionmentioning

confidence: 99%

“…AHCol was salted out by adding NaCl to a final concentration of 2.5 M. The resulting PHCol and AHCol samples were dialyzed against ultrapure water to remove small molecule contaminants and then lyophilized. The purity of the ASCol, PHCol, and AHCol samples was assessed by 5% SDS-PAGE in the presence of 4 M urea (30). Protein molecular mass markers were obtained from APRO Life Science Institute Inc. (Naruto, Japan).…”

Section: Methodsmentioning

confidence: 99%

“…We previously found that actinidain-hydrolyzed collagen (AHCol) of tuna retained its triple-helical structure at pH 4.0 and showed the same thermal stability as that of ASCol, as judged by circular dichroism (CD) spectroscopy. AHCol, however, was found to be essentially monomeric with no cross-linkages, and therefore it provides a unique system for further characterization (30,31).…”

mentioning

confidence: 99%

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Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

Kunii

Morimoto

Nagai

et al. 2010

Journal of Biological Chemistry

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We investigated the ability of type I collagen telopeptides to bind neighboring collagen molecules, which is thought to be the initial event in fibrillogenesis. Limited hydrolysis by actinidain protease produced monomeric collagen, which consisted almost entirely of ␣1 and ␣2 chains. As seen with ultrahigh resolution scanning electron microscopy, actinidain-hydrolyzed collagen exhibited unique self-assembly, as if at an intermediate stage, and formed a novel suprastructure characterized by poor fibrillogenesis. Then, the N-and C-terminal sequences of chicken type I collagen hydrolyzed by actinidain or pepsin were determined by Edman degradation and de novo sequence analysis with matrix-assisted laser desorption ionization-tandem time-of-flight mass spectrometry, respectively. In the C-telopeptide region of the ␣1 1031 . We demonstrated that a synthetic nonapeptide mimicking the ␣1 C-terminal sequence including GFD weakly inhibited the self-assembly of pepsin-hydrolyzed collagen, whereas it remarkably accelerated that of actinidain-hydrolyzed collagen. We conclude that the specific GFD sequence of the C-telopeptide of the ␣1 chain plays a crucial role in stipulating collagen suprastructure and in subsequent fibril formation.Type I collagen is the most abundant protein in connective tissue of all vertebrates. It forms highly ordered fibrils that are generally thought to provide mechanical strength and regulate cell function (1-5). Collagen is formed from tightly interwoven heterotrimers of two ␣1 chains and one ␣2 chain in a triplehelical coiled-coil structure. The triple helix consisting of GlyXaa-Yaa repeats is ϳ1,000 amino acid residues in length and is resistant to proteolysis except for specific collagenases that can cleave the helix (6, 7). The high content of 4-hydroxyproline in the Yaa position stabilizes the triple-helical structure (8, 9).Observations of in vitro collagen fibril formation suggest that the collagen molecule has sufficient structural information to assemble spontaneously under suitable conditions. This structural information has been partially revealed by atomic force microscopy, electron microscopy, spectroscopic analysis, and x-ray diffraction (10 -15). From this information, it appears that the telopeptide regions play an important role in the rate of fibril formation and in azimuthal and lateral growth of fibrils. Indeed, fibril formation of pepsin-hydrolyzed collagen (PHCol) 2 that has been partially hydrolyzed at the N-and C-telopeptide domains progresses more slowly than that of acidsoluble collagen (ASCol) (16,17). The recognition and association of collagen N-and C-telopeptides have been partly demonstrated in vitro (18 -25). The results imply that the Nand C-telopeptide regions are required to "seed" the interaction between collagen molecules. It was also concluded that the triple-helical structure is essential for fibril formation (4, 26).Our experimental approach to understand the mechanism of fibril formation was to investigate type I collagen that had been partially hydro...

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Section: Discussionsupporting

confidence: 94%

Section: Methodsmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

Kunii

Morimoto

Nagai

et al. 2010

Journal of Biological Chemistry

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Enzymes in Meat Processing

Lantto

Kruus

Puolanne

et al. 2009

Enzymes in Food Technology

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Collagen based electrospun materials for skin wounds treatment

Hernández-Rangel

Martín‐Martínez

2021

J Biomedical Materials Res

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Materials used for wound care have evolved from simple covers to functional wound dressings with bioactive properties. Electrospun nanofibers show great similarity to the natural fibrillar structure of skin extracellular matrix (ECM); therefore, by mimic, the morphology of ECM, nanofibers show high potential for facilitating the healing of skin injuries. Besides morphology, scaffold composition is another important parameter in the production of bioactive wound dressings. Collagen type I is the main structural protein of skin ECM is biocompatible, biodegradable, and its extraction from animal sources is relatively simple. The fabrication of electrospun wound dressings based on collagen and its blends have been studied for skin tissue engineering applications. This review focus on the new advances of collagen electrospun materials for skin wound treatment. It summarizes the recent research on pristine collagen, collagen blends, and collagen surface modifications on nanofibers mats. Finally, the strategies for three‐dimensional nanofibers production will also be discussed.

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Preparation and Structural Analysis of Actinidain-processed Atelocollagen of Yellowfin Tuna (Thunnus albacares)

Cited by 15 publications

References 31 publications

Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

Actinidain-hydrolyzed Type I Collagen Reveals a Crucial Amino Acid Sequence in Fibril Formation

Enzymes in Meat Processing

Collagen based electrospun materials for skin wounds treatment

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