Distribution, Typical Structure and Self-Assembly Properties of Collagen from Fish Skin and Bone

The source and type of collagen are crucial to its application, and both play a decisive role. Collagen was prepared from both tilapia skin and bone and skate skin and cartilage, named as CI-TI-s, CI-TI-b, CI-SK-s, and CII-SK-c, respectively. Types, distributions, structures, and self-assembly of co...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2023-09, Vol.28 (18), p.6529
Main Authors: Zhang, Xuening, Wang, Jie, Zhang, Qian, Fan, Yan, Zhang, Hongwei, Ahmad, Khurshid, Hou, Hu
Format: Article
Language:English
Subjects:
Amino acids
Bones
Cartilage
Collagen
Denaturation
Discriminant analysis
Ethylenediaminetetraacetic acid
Fishes
Peptides
Proteins
self-assembly
Skin
Spectrum analysis
structure
Sturgeon
Tendons
Tilapia
unique peptide
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Summary:The source and type of collagen are crucial to its application, and both play a decisive role. Collagen was prepared from both tilapia skin and bone and skate skin and cartilage, named as CI-TI-s, CI-TI-b, CI-SK-s, and CII-SK-c, respectively. Types, distributions, structures, and self-assembly of collagen were studied. It showed that yellow collagen fibers from skin arranged longitudinally, while collagen fibers from skate cartilages displayed varying colors. CI-TI-s, CI-TI-b, CI-SK-s, and CII-SK-c showed the typical amide A (3316–3336 cm−1) and amide B (2929–2948 cm−1) in FTIR spectra. CI-TI-b and CII-SK-c showed 218–229 nm of UV absorption, 11.56–12.20 Å of d values in XRD, and 0.12–0.14 of Rpn values in CD. The thermal denaturation temperatures of CI-TI-s and CI-SK-s were 30.7 and 20.6 °C, respectively. The self-assembly of CI-TI-s and CII-SK-c were maximum at pH 7.2 and 7.4–7.6, respectively. The unique collagen peptides of tilapia and skate were GPSGPQGAVGATGPK, PAMPVPGPMGPMGPR, SPAMPVPGPMGPMGPR, GESGPSGPAGPAGPAGVR, SSGPPVPGPIGPMGPR, GLTGPIGVPGPPGAQGEK, GLAGPQGPR, and GLSGDPGVQGIK, respectively. The unique peptides of type I and type II collagen were GPTGEIGATGLAGAR, GVLGLTGMR, LGLTGMR, GEPGAAGPAGPSGPMGPR, SSGPPVPGPIGPMGPR, and GLSGDPGVQGIK, respectively.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules28186529