Part:BBa_K3672004

SILY，collagen I targeting probe

DS-GAG utilized a peptide sequence derived from the collagen I platelet receptor [RRANAALKAGELYKSILYGC (SILY); Kd: 0.86 μM] DS-GAG modulated collagen fibril organization. It is likely that the DS-GAG also had protective effects for collagens against MMP-mediated degradation by blocking MMP binding sites. In addition, DS facilitated cell proliferation by helping FGF receptors dimerize, since N-acetylgalactosamine (GalNAc) and iduronate (IdoA) can interact with FGFs (FGF-2 and FGF-10) and its receptor, FGFR2-IIIb. Further investigation of the original sequence of SILY revealed that only GELYKCILY was responsible for the collagen binding ability

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

References

1. Stuart K, Paderi J, Snyder PW, Freeman L, Panitch A. Collagen-Binding Peptidoglycans Inhibit MMP Mediated Collagen Degradation and Reduce Dermal Scarring. PLoS ONE. 2011;6:e22139.
2. Geng YQ, McQuillan D, Roughley PJ. SLRP Interaction can protect collagen fibrils from cleavage by collagenases. Matrix Biol. 2006;25:484–491.
3. Paderi JE, Sistiabudi R, Ivanisevic A, Panitch A. Collagen-Binding Peptidoglycans: A Biomimetic Approach to Modulate Collagen Fibrillogenesis for Tissue Engineering Applications. Tissue Eng Part A. 2009;15:2991–2999.
4. [4]Penc SF, Pomahac B, Winkler T, Dorschner RA, Eriksson E, Herndon M, Gallo RL. Dermatan Sulfate released after injury is a potent promoter of fibroblast growth factor-2 function. J Biol Chem. 1998;273:28116–28121.
5. Radek KA, Taylor KR, Gallo RL. FGF-10 and specific structural elements of dermatan sulfate size and sulfation promote maximal keratinocyte migration and cellular proliferation. Wound Repair and Regeneration. 2009;17:118–126.