Abstract:The unique sequence of the α‐chain is the structural cornerstone of the collagen triple helix that dictates its conformation and molecular behavior. In this study, collagen‐like peptides of varying sequence characteristics were designed to elucidate the role of Ser (polar residues), Ala (non‐polar residues), and Arg/Glu (ionizable residues) in the formation, kinetics, and stability of the triple helix, and its self‐assembly behavior. We found that the introduction of other common amino acids in (Gly‐Hyp‐Pro)n … Show more
“…Eventually, the CD signal stabilizes, indicating the complete dissociation of the collagen triple helix structure. 35,36 A derivative analysis of the CD thermal transition curve determined that the denaturation temperature of natural bovine tendon collagen is approximately 43 1C. Thus, this study selected 43 1C as the heat treatment temperature for collagen triple helix dissociation.…”
Section: Degree Of Triple Helix Dissociation In Collagen Samplesmentioning
Collagen plays a crucial role in cancer development and migration. However, the impact of changes in collagen molecular structure on its interaction with cancer cells remains unclear. In this study,...
“…Eventually, the CD signal stabilizes, indicating the complete dissociation of the collagen triple helix structure. 35,36 A derivative analysis of the CD thermal transition curve determined that the denaturation temperature of natural bovine tendon collagen is approximately 43 1C. Thus, this study selected 43 1C as the heat treatment temperature for collagen triple helix dissociation.…”
Section: Degree Of Triple Helix Dissociation In Collagen Samplesmentioning
Collagen plays a crucial role in cancer development and migration. However, the impact of changes in collagen molecular structure on its interaction with cancer cells remains unclear. In this study,...
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